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Journal articles on the topic 'PACSIN2'

Author: Grafiati
Published: 1 April 2023

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1

Zudeh, Giulia, Raffaella Franca, Marianna Lucafò, Erik J. Bonten, Matteo Bramuzzo, Riccardo Sgarra, Cristina Lagatolla, et al. "PACSIN2as a modulator of autophagy and mercaptopurine cytotoxicity: mechanisms in lymphoid and intestinal cells." Life Science Alliance 6, no. 3 (January 3, 2023): e202201610. http://dx.doi.org/10.26508/lsa.202201610.

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PACSIN2 variants are associated with gastrointestinal effects of thiopurines and thiopurine methyltransferase activity through an uncharacterized mechanism that is postulated to involve autophagy. This study aims to clarify the role of PACSIN2 in autophagy and in thiopurine cytotoxicity in leukemic and intestinal models. Higher autophagy and lower PACSIN2 levels were observed in inflamed compared with non-inflamed colon biopsies of inflammatory bowel disease pediatric patients at diagnosis. PACSIN2 was identified as an inhibitor of autophagy, putatively through inhibition of autophagosome formation by a protein–protein interaction with LC3-II, mediated by a LIR motif. Moreover, PACSIN2 resulted a modulator of mercaptopurine-induced cytotoxicity in intestinal cells, suggesting that PACSIN2-regulated autophagy levels might influence thiopurine sensitivity. However, PACSIN2 modulates cellular thiopurine methyltransferase activity via mechanisms distinct from its modulation of autophagy.
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2

Nishimura, Tamako, and Shiro Suetsugu. "Super-resolution analysis of PACSIN2 and EHD2 at caveolae." PLOS ONE 17, no. 7 (July 14, 2022): e0271003. http://dx.doi.org/10.1371/journal.pone.0271003.

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Caveolae are plasma membrane invaginations that play important roles in both endocytosis and membrane tension buffering. Typical caveolae have invaginated structures with a high-density caveolin assembly. Membrane sculpting proteins, including PACSIN2 and EHD2, are involved in caveolar biogenesis. PACSIN2 is an F-BAR domain-containing protein with a membrane sculpting ability that is essential for caveolar shaping. EHD2 is also localized at caveolae and involved in their stability. However, the spatial relationship between PACSIN2, EHD2, and caveolin has not yet been investigated. We observed the single-molecule localizations of PACSIN2 and EHD2 relative to caveolin-1 in three-dimensional space. The single-molecule localizations were grouped by their proximity localizations into the geometric structures of blobs. In caveolin-1 blobs, PACSIN2, EHD2, and caveolin-1 had overlapped spatial localizations. Interestingly, the mean centroid of the PACSIN2 F-BAR domain at the caveolin-1 blobs was closer to the plasma membrane than those of EHD2 and caveolin-1, suggesting that PACSIN2 is involved in connecting caveolae to the plasma membrane. Most of the blobs with volumes typical of caveolae had PACSIN2 and EHD2, in contrast to those with smaller volumes. Therefore, PACSIN2 and EHD2 are apparently localized at typically sized caveolae.
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3

Gusmira, Aini, Kazuhiro Takemura, Shin Yong Lee, Takehiko Inaba, Kyoko Hanawa-Suetsugu, Kayoko Oono-Yakura, Kazuma Yasuhara, Akio Kitao, and Shiro Suetsugu. "Regulation of caveolae through cholesterol-depletion-dependent tubulation mediated by PACSIN2." Journal of Cell Science 133, no. 19 (September 2, 2020): jcs246785. http://dx.doi.org/10.1242/jcs.246785.

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ABSTRACTThe membrane-shaping ability of PACSIN2 (also known as syndapin II), which is mediated by its F-BAR domain, has been shown to be essential for caveolar morphogenesis, presumably through the shaping of the caveolar neck. Caveolar membranes contain abundant cholesterol. However, the role of cholesterol in PACSIN2-mediated membrane deformation remains unclear. Here, we show that the binding of PACSIN2 to the membrane can be negatively regulated by cholesterol. We prepared reconstituted membranes based on the lipid composition of caveolae. The reconstituted membrane with cholesterol had a weaker affinity for the F-BAR domain of PACSIN2 than a membrane without cholesterol. Consistent with this, upon depletion of cholesterol from the plasma membrane, PACSIN2 localized at tubules that had caveolin-1 at their tips, suggesting that cholesterol inhibits membrane tubulation mediated by PACSIN2. The tubules induced by PACSIN2 could be representative of an intermediate of caveolae endocytosis. Consistent with this, the removal of caveolae from the plasma membrane upon cholesterol depletion was diminished in the PACSIN2-deficient cells. These data suggest that PACSIN2-mediated caveolae internalization is dependent on the amount of cholesterol, providing a mechanism for cholesterol-dependent regulation of caveolae.This article has an associated First Person interview with the first author of the paper.
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4

Popov, Sergei, Elena Popova, Michio Inoue, Yuanfei Wu, and Heinrich Göttlinger. "HIV-1 gag recruits PACSIN2 to promote virus spreading." Proceedings of the National Academy of Sciences 115, no. 27 (June 11, 2018): 7093–98. http://dx.doi.org/10.1073/pnas.1801849115.

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The p2b domain of Rous sarcoma virus (RSV) Gag and the p6 domain of HIV-1 Gag contain late assembly (L) domains that engage the ESCRT membrane fission machinery and are essential for virus release. We now show that the PPXY-type RSV L domain specifically recruits the BAR domain protein PACSIN2 into virus-like particles (VLP), in addition to the NEDD4-like ubiquitin ligase ITCH and ESCRT pathway components such as TSG101. PACSIN2, which has been implicated in the remodeling of cellular membranes and the actin cytoskeleton, is also recruited by HIV-1 p6 independent of its ability to engage the ESCRT factors TSG101 or ALIX. Moreover, PACSIN2 is robustly recruited by NEDD4-2s, a NEDD4-like ubiquitin ligase capable of rescuing HIV-1 budding defects. The NEDD4-2s–induced incorporation of PACSIN2 into VLP correlated with the formation of Gag-ubiquitin conjugates, indicating that PACSIN2 binds ubiquitin. Although PACSIN2 was not required for a single cycle of HIV-1 replication after infection with cell-free virus, HIV-1 spreading was nevertheless severely impaired in T cell lines and primary human peripheral blood mononuclear cells depleted of PACSIN2. HIV-1 spreading could be restored by reintroduction of wild-type PACSIN2, but not of a SH3 domain mutant unable to interact with the actin polymerization regulators WASP and N-WASP. Overall, our observations indicate that PACSIN2 promotes the cell-to-cell spreading of HIV-1 by connecting Gag to the actin cytoskeleton.
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5

Giannini, Silvia, Markus Bender, Fred G. Pluthero, Hilary Christensen, Richard Leung, Richard W. Lo, Jan Kormann, Markus Plomann, Walter H. A. Kahr, and Hervé Falet. "Dynamin 2 (DNM2) and PACSIN2 Regulate Megakaryocyte Demarcation Membrane System Formation and Platelet Production in Concert." Blood 126, no. 23 (December 3, 2015): 419. http://dx.doi.org/10.1182/blood.v126.23.419.419.

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Abstract Blood platelets are produced in the bone marrow by megakaryocytes (MKs) in a process that requires extensive intracellular membrane rearrangements. These include the formation of the demarcation membrane system (DMS), the surface-connected membrane extension that invaginates into the cell body and further develops to provide membranes for future platelets. The precise molecular mechanisms responsible for these unique membrane rearrangements remain poorly understood. We have recently shown that Dnm2fl/fl Pf4-Cre mice specifically lacking the large GTPase dynamin 2 (DNM2) in MKs develop severe macrothrombocytopenia due to impaired receptor-mediated endocytosis (RME) (Bender, Giannini et al. Blood. 2015;125(6):1014-1024). Specifically, Dnm2fl/fl Pf4-Cre MKs accumulate arrested endocytic clathrin-coated vesicles that obstruct DMS formation. The actin nucleating factor Arp2/3 complex and polymerized actin clustered with clathrin at sites of impaired RME in Dnm2fl/fl Pf4-Cre MKs. We hypothesized that a DNM2 partner recruits actin-regulatory proteins at sites of RME and investigated the contribution of the F-BAR protein PACSIN2, an internal component of the initiating DMS (Jurak Begonja, Pluthero et al. Blood. 2015;126(1):80-88), in DMS formation and platelet production, as PACSIN2 interacts with DNM2 and actin-regulatory proteins such as N-WASP and filamin A (FlnA). Pacsin2-/- mice developed mild thrombocytopenia with slightly enlarged and shallow platelets. The DMS appeared less well defined and platelet territories were not readily visualized in Pacsin2-/- MKs. Pacsin2-/- Dnm2fl/fl Pf4-Cre mice lacking both PACSIN2 and DNM2 in MKs were further generated to determine the contribution of PACSIN2 in clathrin and actin clustering in Dnm2fl/fl Pf4-Cre MKs. Strikingly, PACSIN2 genetic deletion significantly improved the severe thrombocytopenia of Dnm2fl/fl Pf4-Cre mice. Specifically, PACSIN2 deletion abrogated the accumulation of clathrin and actin clusters, thereby unclogging DMS formation, which appeared as elongated maze-like membrane tubules in Pacsin2-/- Dnm2fl/fl Pf4-Cre MKs. Our results show that DNM2 terminates PACSIN2-dependent actin polymerization that accompanies RME, thereby allowing membrane rearrangements required for DMS formation. Disclosures No relevant conflicts of interest to declare.
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6

Jönsson, Terese, Fred G. Pluthero, Antonija Jurak Begonja, Jan Kormann, Mélanie Demers, Denisa D. Wagner, Markus Plomann, John H. Hartwig, Walter H. Kahr, and Hervé Falet. "The F-BAR Protein PACSIN2 Regulates Platelet Intracellular Membrane Architecture and in Vivo Hemostatic Functions." Blood 124, no. 21 (December 6, 2014): 4154. http://dx.doi.org/10.1182/blood.v124.21.4154.4154.

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Abstract Proteins of the Bin-amphiphysin-Rvs (BAR) and Fes-CIP4 homology BAR (F-BAR) families bind and deform membranes, promoting in cells tubular invaginations reminiscent of the platelet open canalicular system (OCS) and megakaryocyte (MK) demarcation membrane system (DMS). Here we investigated the role of the F-BAR protein PACSIN2 in platelets and MKs. Spinning disk laser fluorescence confocal microscopy showed that PACSIN2 co-localized with the von Willebrand factor receptor subunit GPIbα at the openings of the OCS in platelets. Endogenous and over-expressed PACSIN2 associated with anastomosing tubular structures reminiscent of the pre-DMS in mouse bone marrow MKs. Pacsin2-null mice had mild thrombocytopenia and polycythemia, MK hyperplasia and splenomegaly. Pacsin2-null mice had a bleeding disorder, as evidenced by significantly prolonged tail bleeding and delayed in vivo thrombus formation following FeCl3 vascular injury, which was normalized by injection of WT platelets. However, Pacsin2-null platelets expressed P-selectin and activated the integrin αIIbβ3 normally in response to stimulation with thrombin and the GPVI-specific collagen-related peptide. In contrast, Pacsin2-null platelets had abnormal flattened morphology, with more and narrower OCS channels on their surface, compared to WT platelets. Together, the data indicate that the F-BAR protein PACSIN2 orchestrates the intracellular membrane architecture of platelets, thereby regulating their in vivo hemostatic functions. Disclosures No relevant conflicts of interest to declare.
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7

Postema, Meagan M., Nathan E. Grega-Larson, Leslie M. Meenderink, and Matthew J. Tyska. "PACSIN2-dependent apical endocytosis regulates the morphology of epithelial microvilli." Molecular Biology of the Cell 30, no. 19 (September 1, 2019): 2515–26. http://dx.doi.org/10.1091/mbc.e19-06-0352.

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Apical microvilli are critical for the homeostasis of transporting epithelia, yet mechanisms that control the assembly and morphology of these protrusions remain poorly understood. Previous studies in intestinal epithelial cell lines suggested a role for the F-BAR domain protein PACSIN2 in normal microvillar assembly. Here we report the phenotype of PACSIN2 KO mice and provide evidence that through its role in promoting apical endocytosis, this molecule plays a role in controlling microvillar morphology. PACSIN2 KO enterocytes exhibit reduced numbers of microvilli and defects in the microvillar ultrastructure, with membranes lifting away from rootlets of core bundles. Dynamin2, a PACSIN2 binding partner, and other endocytic factors were also lost from their normal localization near microvillar rootlets. To determine whether loss of endocytic machinery could explain defects in microvillar morphology, we examined the impact of PACSIN2 KD and endocytosis inhibition on live intestinal epithelial cells. These assays revealed that when endocytic vesicle scission fails, tubules are pulled into the cytoplasm and this, in turn, leads to a membrane-lifting phenomenon reminiscent of that observed at PACSIN2 KO brush borders. These findings lead to a new model where inward forces generated by endocytic machinery on the plasma membrane control the membrane wrapping of cell surface protrusions.
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8

Begonja, Antonija Jurak, Fred G. Pluthero, Worawit Suphamungmee, Silvia Giannini, Hilary Christensen, Richard Leung, Richard W. Lo, et al. "FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets." Blood 126, no. 1 (July 2, 2015): 80–88. http://dx.doi.org/10.1182/blood-2014-07-587600.

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Key PointsThe F-BAR protein PACSIN2 associates with the initiating demarcation membrane system in megakaryocytes. FlnA binding to the PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes, platelets, and in vitro.
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9

Sanderlin, Allen G., Cassandra Vondrak, Arianna J. Scricco, Indro Fedrigo, Vida Ahyong, and Rebecca L. Lamason. "RNAi screen reveals a role for PACSIN2 and caveolins during bacterial cell-to-cell spread." Molecular Biology of the Cell 30, no. 17 (August 2019): 2124–33. http://dx.doi.org/10.1091/mbc.e19-04-0197.

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Listeria monocytogenes is a human bacterial pathogen that disseminates through host tissues using a process called cell-to-cell spread. This critical yet understudied virulence strategy resembles a vesicular form of intercellular trafficking that allows L. monocytogenes to move between host cells without escaping the cell. Interestingly, eukaryotic cells can also directly exchange cellular components via intercellular communication pathways (e.g., trans-endocytosis) using cell–cell adhesion, membrane trafficking, and membrane remodeling proteins. Therefore, we hypothesized that L. monocytogenes would hijack these types of host proteins during spread. Using a focused RNA interference screen, we identified 22 host genes that are important for L. monocytogenes spread. We then found that caveolins (CAV1 and CAV2) and the membrane sculpting F-BAR protein PACSIN2 promote L. monocytogenes protrusion engulfment during spread, and that PACSIN2 specifically localizes to protrusions. Overall, our study demonstrates that host intercellular communication pathways may be coopted during bacterial spread and that specific trafficking and membrane remodeling proteins promote bacterial protrusion resolution.
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10

Chitu, Violeta, and E. Richard Stanley. "PACSIN2: a BAR-rier forming the megakaryocyte DMS." Blood 126, no. 1 (July 2, 2015): 5–6. http://dx.doi.org/10.1182/blood-2015-04-639450.

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11

Cousin, Hélène, Douglas W. DeSimone, and Dominique Alfandari. "PACSIN2 regulates cell adhesion during gastrulation in Xenopus laevis." Developmental Biology 319, no. 1 (July 2008): 86–99. http://dx.doi.org/10.1016/j.ydbio.2008.04.007.

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12

Cousin, Hélène, Alban Gaultier, Christian Bleux, Thierry Darribère, and Dominique Alfandari. "PACSIN2 Is a Regulator of the Metalloprotease/Disintegrin ADAM13." Developmental Biology 227, no. 1 (November 2000): 197–210. http://dx.doi.org/10.1006/dbio.2000.9871.

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13

Cousin, Hélène, Alban Gaultier, Christian Bleux, Thierry Darribère, and Dominique Alfandari. "PACSIN2 Is a Regulator of the Metalloprotease/Disintegrin ADAM13." Developmental Biology 229, no. 2 (January 2001): 568. http://dx.doi.org/10.1006/dbio.2001.0128.

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14

Kostan, Julius, Ulrich Salzer, Albina Orlova, Imre Törö, Vesna Hodnik, Yosuke Senju, Juan Zou, et al. "Direct interaction of actin filaments with F ‐ BAR protein pacsin2." EMBO reports 15, no. 11 (September 12, 2014): 1154–62. http://dx.doi.org/10.15252/embr.201439267.

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15

Van Duyne, Rachel, and Eric O. Freed. "HIV-1 packs in PACSIN2 for cell-to-cell spread." Proceedings of the National Academy of Sciences 115, no. 27 (June 20, 2018): 6885–87. http://dx.doi.org/10.1073/pnas.1808821115.

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16

Stocco, Gabriele, Wenjian Yang, Kristine R. Crews, William E. Thierfelder, Giuliana Decorti, Margherita Londero, Raffaella Franca, et al. "PACSIN2 polymorphism influences TPMT activity and mercaptopurine-related gastrointestinal toxicity." Human Molecular Genetics 21, no. 21 (July 30, 2012): 4793–804. http://dx.doi.org/10.1093/hmg/dds302.

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17

Senju, Y., Y. Itoh, K. Takano, S. Hamada, and S. Suetsugu. "Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting." Journal of Cell Science 124, no. 12 (May 24, 2011): 2032–40. http://dx.doi.org/10.1242/jcs.086264.

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18

Chandrasekaran, Ramyavardhanee, Anne K. Kenworthy, and D. Borden Lacy. "Clostridium difficile Toxin A Undergoes Clathrin-Independent, PACSIN2-Dependent Endocytosis." PLOS Pathogens 12, no. 12 (December 12, 2016): e1006070. http://dx.doi.org/10.1371/journal.ppat.1006070.

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19

Franca, Raffaella, Gabriele Stocco, Diego Favretto, Nagua Giurici, Irene del Rizzo, Franco Locatelli, Luciana Vinti, et al. "PACSIN2 rs2413739 influence on thiopurine pharmacokinetics: validation studies in pediatric patients." Pharmacogenomics Journal 20, no. 3 (December 3, 2019): 415–25. http://dx.doi.org/10.1038/s41397-019-0130-0.

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20

de Kreuk, Bart-Jan, Eloise C. Anthony, Dirk Geerts, and Peter L. Hordijk. "The F-BAR Protein PACSIN2 Regulates Epidermal Growth Factor Receptor Internalization." Journal of Biological Chemistry 287, no. 52 (November 5, 2012): 43438–53. http://dx.doi.org/10.1074/jbc.m112.391078.

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21

Modregger, J., B. Ritter, B. Witter, M. Paulsson, and M. Plomann. "All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis." Journal of Cell Science 113, no. 24 (December 15, 2000): 4511–21. http://dx.doi.org/10.1242/jcs.113.24.4511.

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The PACSINs are a family of cytoplasmic phosphoproteins that play a role in vesicle formation and transport. We report the cloning and cDNA sequencing of PACSIN 3 and the analysis of all three PACSIN isoforms with regard to tissue distribution, ligand binding properties and influence on endocytosis. PACSIN 3 differs from the other family members in having a short proline-rich region and lacking asparagine-proline-phenylalanine motifs. In contrast to the neurospecific PACSIN 1 and the ubiquitously expressed PACSIN 2, PACSIN 3 is mainly detected in lung and muscle tissues. All isoforms potentially oligomerize and bind to dynamin, synaptojanin 1 and N-WASP via their Src homology 3 domains. The PACSIN proteins colocalize with dynamin, but not with clathrin, implying a specific role with a distinct subpopulation of dynamin at defined cellular sites. Transferrin endocytosis is blocked in a dose-dependent manner in cells overexpressing the PACSIN variants, but the inhibitory effect can be abolished by mutating specific amino acid residues in the Src homology 3 domains. These characteristics of the PACSIN protein family suggest a general function in recruitment of the interacting proteins to sites of endocytosis.
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22

Tirozzi, Alfonsina, Miriam Shasa Quiccione, Chiara Cerletti, Maria Benedetta Donati, Giovanni de Gaetano, Licia Iacoviello, and Alessandro Gialluisi. "A Multi-Trait Association Analysis of Brain Disorders and Platelet Traits Identifies Novel Susceptibility Loci for Major Depression, Alzheimer’s and Parkinson’s Disease." Cells 12, no. 2 (January 6, 2023): 245. http://dx.doi.org/10.3390/cells12020245.

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Among candidate neurodegenerative/neuropsychiatric risk-predictive biomarkers, platelet count, mean platelet volume and platelet distribution width have been associated with the risk of major depressive disorder (MDD), Alzheimer’s disease (AD) and Parkinson’s disease (PD) through epidemiological and genomic studies, suggesting partial co-heritability. We exploited these relationships for a multi-trait association analysis, using publicly available summary statistics of genome-wide association studies (GWASs) of all traits reported above. Gene-based enrichment tests were carried out, as well as a network analysis of significantly enriched genes. We analyzed 4,540,326 single nucleotide polymorphisms shared among the analyzed GWASs, observing 149 genome-wide significant multi-trait LD-independent associations (p < 5 × 10−8) for AD, 70 for PD and 139 for MDD. Among these, 27 novel associations were detected for AD, 34 for PD and 40 for MDD. Out of 18,781 genes with annotated variants within ±10 kb, 62 genes were enriched for associations with AD, 70 with PD and 125 with MDD (p < 2.7 × 10−6). Of these, seven genes were novel susceptibility loci for AD (EPPK1, TTLL1, PACSIN2, TPM4, PIF1, ZNF689, AZGP1P1), two for PD (SLC26A1, EFNA3) and two for MDD (HSPH1, TRMT61A). The resulting network showed a significant excess of interactions (enrichment p = 1.0 × 10−16). The novel genes that were identified are involved in the organization of cytoskeletal architecture (EPPK1, TTLL1, PACSIN2, TPM4), telomere shortening (PIF1), the regulation of cellular aging (ZNF689, AZGP1P1) and neurodevelopment (EFNA3), thus, providing novel insights into the shared underlying biology of brain disorders and platelet parameters.
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23

Dumont, Vincent, Tuomas A. Tolvanen, Sara Kuusela, Hong Wang, Tuula A. Nyman, Sonja Lindfors, Jukka Tienari, et al. "PACSIN2 accelerates nephrin trafficking and is up‐regulated in diabetic kidney disease." FASEB Journal 31, no. 9 (September 2017): 3978–90. http://dx.doi.org/10.1096/fj.201601265r.

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24

Roberts, Rebecca L., Mary C. Wallace, Margien L. Seinen, Krupa Krishnaprasad, Angela Chew, Ian Lawrance, Ruth Prosser, et al. "PACSIN2 Does Not Influence Thiopurine-Related Toxicity In Patients With Inflammatory Bowel Disease." American Journal of Gastroenterology 109, no. 6 (June 2014): 925–27. http://dx.doi.org/10.1038/ajg.2014.89.

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Roberts, Rebecca L., Mary C. Wallace, Margien L. Seinen, Krupa Krishnaprasad, Angela Chew, Ian Lawrance, Ruth Prosser, et al. "Corrigendum: PACSIN2 Does Not Influence Thiopurine-Related Toxicity in Patients With Inflammatory Bowel Disease." American Journal of Gastroenterology 110, no. 1 (January 2015): 204. http://dx.doi.org/10.1038/ajg.2014.322.

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26

de Kreuk, B. J., M. Nethe, M. Fernandez-Borja, E. C. Anthony, P. J. Hensbergen, A. M. Deelder, M. Plomann, and P. L. Hordijk. "The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration." Journal of Cell Science 124, no. 14 (June 21, 2011): 2375–88. http://dx.doi.org/10.1242/jcs.080630.

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27

Senju, Y., E. Rosenbaum, C. Shah, S. Hamada-Nakahara, Y. Itoh, K. Yamamoto, K. Hanawa-Suetsugu, O. Daumke, and S. Suetsugu. "Phosphorylation of PACSIN2 by protein kinase C triggers the removal of caveolae from the plasma membrane." Journal of Cell Science 128, no. 15 (June 19, 2015): 2766–80. http://dx.doi.org/10.1242/jcs.167775.

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28

Senju, Yosuke, and Shiro Suetsugu. "Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II." BioArchitecture 5, no. 5-6 (December 2, 2015): 70–77. http://dx.doi.org/10.1080/19490992.2015.1128604.

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29

Novikova, Svetlana E., Natalia A. Soloveva, Tatiana E. Farafonova, Olga V. Tikhonova, Pao-Chi Liao, and Victor G. Zgoda. "Proteomic Signature of Extracellular Vesicles for Lung Cancer Recognition." Molecules 26, no. 20 (October 12, 2021): 6145. http://dx.doi.org/10.3390/molecules26206145.

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The proteins of extracellular vesicles (EVs) that originate from tumors reflect the producer cells’ proteomes and can be detected in biological fluids. Thus, EVs provide proteomic signatures that are of great interest for screening and predictive cancer diagnostics. By applying targeted mass spectrometry with stable isotope-labeled peptide standards, we assessed the levels of 28 EV-associated proteins, including the conventional exosome markers CD9, CD63, CD81, CD82, and HSPA8, in vesicles derived from the lung cancer cell lines NCI-H23 and A549. Furthermore, we evaluated the detectability of these proteins and their abundance in plasma samples from 34 lung cancer patients and 23 healthy volunteers. The abundance of TLN1, TUBA4A, HSPA8, ITGB3, TSG101, and PACSIN2 in the plasma of lung cancer patients was measured using targeted mass spectrometry and compared to that in plasma from healthy volunteers. The most diagnostically potent markers were TLN1 (AUC, 0.95), TUBA4A (AUC, 0.91), and HSPA8 (AUC, 0.88). The obtained EV proteomic signature allowed us to distinguish between the lung adenocarcinoma and squamous cell carcinoma histological types. The proteomic cargo of the extracellular vesicles represents a promising source of potential biomarkers.
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Morén, Björn, Claudio Shah, Mark T. Howes, Nicole L. Schieber, Harvey T. McMahon, Robert G. Parton, Oliver Daumke, and Richard Lundmark. "EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization." Molecular Biology of the Cell 23, no. 7 (April 2012): 1316–29. http://dx.doi.org/10.1091/mbc.e11-09-0787.

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Eps15 homology domain–containing 2 (EHD2) belongs to the EHD-containing protein family of dynamin-related ATPases involved in membrane remodeling in the endosomal system. EHD2 dimers oligomerize into rings on highly curved membranes, resulting in stimulation of the intrinsic ATPase activity. In this paper, we report that EHD2 is specifically and stably associated with caveolae at the plasma membrane and not involved in clathrin-mediated endocytosis or endosomal recycling, as previously suggested. EHD2 interacts with pacsin2 and cavin1, and ordered membrane assembly of EHD2 is dependent on cavin1 and caveolar integrity. While the EHD of EHD2 is dispensable for targeting, we identified a loop in the nucleotide-binding domain that, together with ATP binding, is required for caveolar localization. EHD2 was not essential for the formation or shaping of caveolae, but high levels of EHD2 caused distortion and loss of endogenous caveolae. Assembly of EHD2 stabilized and constrained caveolae to the plasma membrane to control turnover, and depletion of EHD2, resulting in endocytic and more dynamic and short-lived caveolae. Thus, following the identification of caveolin and cavins, EHD2 constitutes a third structural component of caveolae involved in controlling the stability and turnover of this organelle.
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31

Senju, Yosuke, and Shiro Suetsugu. "3P197 The role of F-BAR protein pacsin2 in the formation of caveolae(Cell biology,The 48th Annual Meeting of the Biophysical Society of Japan)." Seibutsu Butsuri 50, supplement2 (2010): S179. http://dx.doi.org/10.2142/biophys.50.s179_5.

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32

Shimada, Atsushi, Kazunori Takano, Mikako Shirouzu, Kyoko Hanawa-Suetsugu, Takaho Terada, Kiminori Toyooka, Takashi Umehara, Masaki Yamamoto, Shigeyuki Yokoyama, and Shiro Suetsugu. "Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II." FEBS Letters 584, no. 6 (February 24, 2010): 1111–18. http://dx.doi.org/10.1016/j.febslet.2010.02.058.

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33

Gong, Yan, Yuebo Zhang, Biao Li, Yu Xiao, Qinghua Zeng, Kang Xu, Yehui Duan, Jianhua He, and Haiming Ma. "Insight into Liver lncRNA and mRNA Profiling at Four Developmental Stages in Ningxiang Pig." Biology 10, no. 4 (April 8, 2021): 310. http://dx.doi.org/10.3390/biology10040310.

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Ningxiang pigs, a fat-type pig, are native to Ningxiang County in Hunan Province, with thousands of years of breeding history. This study aims to explore the expression profiles and functional networks on messenger RNAs (mRNAs) and long non-coding RNAs (lncRNAs) in the liver. Liver tissue of Ningxiang piglets was collected at 30, 90, 150, and 210 days after birth (four development stages), and the mRNA and lncRNA expression was profiled. Compared to mRNA and lncRNA expression profiles, most differentially expressed mRNAs (DEmRNAs) were upregulated at 30 days; however, most DElncRNAs were downregulated at 210 days. Via Short Time-series Expression Miner (STEM) analysis and weighted gene co-expression network analysis (WGCNA), a complex interaction between mRNAs and lncRNAs was identified, indicating that lncRNAs may be a critical regulatory element for mRNAs. One module of genes in particular (module profile 4) was related to fibril organization, vasculogenesis, GTPase activator activity, and regulation of kinase activity. The mRNAs and lncRNAs in module profile 4 had a similar pattern of expression, indicating that they have functional and regulatory relationships. Only CAV1, PACSIN2, and CDC42 in the particular mRNA profile 4 were the target genes of lncRNAs in that profile, which shows the possible regulatory relationship between lncRNAs and mRNAs. The expression of these genes and lncRNAs in profile 4 was the highest at 30 days, and it is believed that these RNAs may play a critical role during the suckling period in order to meet the dietary requirements of piglets. In the lncRNA–mRNA co-expression network, the identified gene hubs and associated lncRNAs were shown to be involved in saccharide, lipid, and glucose metabolism, which may play an important role in the development and health of the liver. This result will lead to further investigation of liver lncRNA functions at various stages of development in Ningxiang pigs.
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34

Jónsson, Terese, Antonija Jurak Begonja, Jan Kormann, Barbara Merkl, Fred Pluthero, Walter H. Kahr, John H. Hartwig, Markus Plomann, and Hervé Falet. "The F-BAR Protein PACSIN 2 Specifically Coats the Anastomosing Intracellular Membrane Systems of Platelets and Megakaryocytes,." Blood 118, no. 21 (November 18, 2011): 3261. http://dx.doi.org/10.1182/blood.v118.21.3261.3261.

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Abstract Abstract 3261 Megakaryocyte (MK) maturation and platelet formation are associated with extensive intracellular membrane rearrangements. However, the cellular proteins and mechanisms responsible for the formation of the platelet open canalicular system (OCS) are unknown. PACSIN 1–3 belong to the novel family of F-BAR domain-containing proteins, which bind and deform membranes, promoting tubular invaginations. Blood platelets and MKs contain the ubiquitously expressed PACSIN 2, but not PACSIN 1 or 3, as evidenced by intracellular flow cytometry and immunoblot analysis. Spinning disk laser fluorescence confocal microscopy revealed a specific association between PACSIN 2 and tubular structures in human platelets. PACSIN 2 did not colocalize with granule or lysosome markers, i.e. CD62P, CD63 and LAMP1, suggesting that it coats the OCS. In mouse MKs, PACSIN 2 was distributed through the cell body and colocalized with the membrane marker, CD61. Immunoprecipitation of PACSIN 2 from human platelet lysates pulled down filamin A (FlnA), a major platelet cytoskeletal protein. The interaction required PACSIN 2 F-BAR domain, as evidenced by in vitro binding assays using recombinant proteins. Mice lacking FlnA in the MK lineage have a severe thrombocytopenia with large platelets (Falet et al, J Exp Med 2010; Jurak Begonja et al, Blood 2011). In contrast to wild type platelets, FlnA-null platelets had diffuse PACSIN 2 staining and abnormal intracellular membrane structures, suggesting that the PACSIN 2-FlnA interaction is necessary for the integrity of the platelet intracellular membrane systems. PACSIN 2-null mice had a mild thrombocytopenia, enlarged spleens and increased spleen megakaryopoiesis. Together, the data shows that PACSIN 2 is expressed in platelets and MKs, where it specifically coats the anastomosing intracellular membrane systems in cooperation with FlnA. Disclosures: No relevant conflicts of interest to declare.
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35

Bai, Xiaoyun, Geng Meng, and Xiaofeng Zheng. "Cloning, purification, crystallization and preliminary X-ray diffraction analysis of mouse PACSIN 3 protein." Acta Crystallographica Section F Structural Biology and Crystallization Communications 68, no. 2 (January 25, 2012): 159–62. http://dx.doi.org/10.1107/s1744309111049116.

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PACSIN-family proteins are cytoplasmic proteins that have vesicle-transport, membrane-dynamics, actin-reorganization and microtubule activities. Here, the N-terminal F-BAR domain of mouse PACSIN 3, which contains 341 amino acids, was successfully cloned, purified and crystallized. The crystal of PACSIN 3 (1–341) diffracted to 2.6 Å resolution and belonged to space groupP21, with unit-cell parametersa= 46.9,b= 54.7,c= 193.7 Å, α = 90, β = 96.9, γ = 90°. These data should provide further information on PACSIN-family protein structures.
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36

Jones, T., W. Yang, W. Evans, and M. Relling. "Using hapmap tools to predict oncology-related phenotypes: TPMT activity vs hapmap SNPs." Journal of Clinical Oncology 24, no. 18_suppl (June 20, 2006): 13035. http://dx.doi.org/10.1200/jco.2006.24.18_suppl.13035.

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13035 Background: Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme responsible for the S-methylation of thiopurines. There are several functional genetic polymorphisms in TPMT activity, which can lead to drug toxicities; however, among individuals with high TPMT activity, a substantial portion of enzymatic variability remains unexplained. B-lymphoblastoid CEPH cell lines have been genotyped at over 2 million single nucleotide polymorphisms (SNPs) as part of the International HapMap project. Therefore, extensive phenotype-genotype association studies can be conducted in these cell lines by systematic determination of cancer-related phenotypes. Methods: We measured the phenotype of TPMT activity in 82 CEPH cell lines. Of these, 53 had expression data available on over 8000 genes from Affymetrix Focus Array technology. We evaluated whether TPMT activity was associated with HapMap SNPs in TPMT (cis SNPs), genome-wide HapMap SNPs (trans SNPs), and level of gene expression using Kruskal-Wallis test and Spearmans rank correlation. Results: We found associations of TPMT activity with four SNPs (p < 0.05) in TPMT (± 100K bp), one of which (rs1142345, p = 0.009) is a known functional SNP responsible for TPMT deficiency. Two other significant SNPs are in linkage disequilibrium with rs1142345. Associations were also found with 1598 trans SNPs across the genome (p < 0.001). TPMT activity was associated with the expression of eight genes (p < 0.0001, FDR <20%). The only overlapping trans gene is PACSIN2, whose expression most significantly correlated with TPMT activity and also contains two significantly predictive trans SNPs. Conclusions: The CEPH cell lines were useful in that a known functional variant, rs1142345, (serving as a positive control) was associated with TPMT activity, and that additional polymorphisms in TPMT and in potentially important trans-acting factors have been identified as possible additional genomic determinants of TPMT activity. Similar experiments with other phenotypes can likewise capitalize on this publicly available resource. With further validation, these studies may lead to discovery of additional candidate polymorphisms that can lead to further optimization of thiopurine therapy in the clinic. No significant financial relationships to disclose.
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Billcliff, Peter G., Christopher J. Noakes, Zenobia B. Mehta, Guanhua Yan, LokHang Mak, Rudiger Woscholski, and Martin Lowe. "OCRL1 engages with the F-BAR protein pacsin 2 to promote biogenesis of membrane-trafficking intermediates." Molecular Biology of the Cell 27, no. 1 (January 2016): 90–107. http://dx.doi.org/10.1091/mbc.e15-06-0329.

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Mutation of the inositol 5-phosphatase OCRL1 causes Lowe syndrome and Dent-2 disease. Loss of OCRL1 function perturbs several cellular processes, including membrane traffic, but the underlying mechanisms remain poorly defined. Here we show that OCRL1 is part of the membrane-trafficking machinery operating at the trans-Golgi network (TGN)/endosome interface. OCRL1 interacts via IPIP27A with the F-BAR protein pacsin 2. OCRL1 and IPIP27A localize to mannose 6-phosphate receptor (MPR)–containing trafficking intermediates, and loss of either protein leads to defective MPR carrier biogenesis at the TGN and endosomes. OCRL1 5-phosphatase activity, which is membrane curvature sensitive, is stimulated by IPIP27A-mediated engagement of OCRL1 with pacsin 2 and promotes scission of MPR-containing carriers. Our data indicate a role for OCRL1, via IPIP27A, in regulating the formation of pacsin 2–dependent trafficking intermediates and reveal a mechanism for coupling PtdIns(4,5)P2 hydrolysis with carrier biogenesis on endomembranes.
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38

Rahman, Md Habibur, Silong Peng, Xiyuan Hu, Chen Chen, Md Rezanur Rahman, Shahadat Uddin, Julian M. W. Quinn, and Mohammad Ali Moni. "A Network-Based Bioinformatics Approach to Identify Molecular Biomarkers for Type 2 Diabetes that Are Linked to the Progression of Neurological Diseases." International Journal of Environmental Research and Public Health 17, no. 3 (February 6, 2020): 1035. http://dx.doi.org/10.3390/ijerph17031035.

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Neurological diseases (NDs) are progressive disorders, the progression of which can be significantly affected by a range of common diseases that present as comorbidities. Clinical studies, including epidemiological and neuropathological analyses, indicate that patients with type 2 diabetes (T2D) have worse progression of NDs, suggesting pathogenic links between NDs and T2D. However, finding causal or predisposing factors that link T2D and NDs remains challenging. To address these problems, we developed a high-throughput network-based quantitative pipeline using agnostic approaches to identify genes expressed abnormally in both T2D and NDs, to identify some of the shared molecular pathways that may underpin T2D and ND interaction. We employed gene expression transcriptomic datasets from control and disease-affected individuals and identified differentially expressed genes (DEGs) in tissues of patients with T2D and ND when compared to unaffected control individuals. One hundred and ninety seven DEGs (99 up-regulated and 98 down-regulated in affected individuals) that were common to both the T2D and the ND datasets were identified. Functional annotation of these identified DEGs revealed the involvement of significant cell signaling associated molecular pathways. The overlapping DEGs (i.e., seen in both T2D and ND datasets) were then used to extract the most significant GO terms. We performed validation of these results with gold benchmark databases and literature searching, which identified which genes and pathways had been previously linked to NDs or T2D and which are novel. Hub proteins in the pathways were identified (including DNM2, DNM1, MYH14, PACSIN2, TFRC, PDE4D, ENTPD1, PLK4, CDC20B, and CDC14A) using protein-protein interaction analysis which have not previously been described as playing a role in these diseases. To reveal the transcriptional and post-transcriptional regulators of the DEGs we used transcription factor (TF) interactions analysis and DEG-microRNAs (miRNAs) interaction analysis, respectively. We thus identified the following TFs as important in driving expression of our T2D/ND common genes: FOXC1, GATA2, FOXL1, YY1, E2F1, NFIC, NFYA, USF2, HINFP, MEF2A, SRF, NFKB1, USF2, HINFP, MEF2A, SRF, NFKB1, PDE4D, CREB1, SP1, HOXA5, SREBF1, TFAP2A, STAT3, POU2F2, TP53, PPARG, and JUN. MicroRNAs that affect expression of these genes include mir-335-5p, mir-16-5p, mir-93-5p, mir-17-5p, mir-124-3p. Thus, our transcriptomic data analysis identifies novel potential links between NDs and T2D pathologies that may underlie comorbidity interactions, links that may include potential targets for therapeutic intervention. In sum, our neighborhood-based benchmarking and multilayer network topology methods identified novel putative biomarkers that indicate how type 2 diabetes (T2D) and these neurological diseases interact and pathways that, in the future, may be targeted for treatment.
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39

Cuajungco, Math P., Christian Grimm, Kazuo Oshima, Dieter D'hoedt, Bernd Nilius, Arjen R. Mensenkamp, René J. M. Bindels, Markus Plomann, and Stefan Heller. "PACSINs Bind to the TRPV4 Cation Channel." Journal of Biological Chemistry 281, no. 27 (April 20, 2006): 18753–62. http://dx.doi.org/10.1074/jbc.m602452200.

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40

Sumoy, Lauro, Raquel Pluvinet, Nuria Andreu, Xavier Estivill, and Mònica Escarceller. "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family." Gene 262, no. 1-2 (January 2001): 199–205. http://dx.doi.org/10.1016/s0378-1119(00)00531-x.

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41

Goh, Shih Lin, Qi Wang, Laura J. Byrnes, and Holger Sondermann. "Versatile Membrane Deformation Potential of Activated Pacsin." PLoS ONE 7, no. 12 (December 7, 2012): e51628. http://dx.doi.org/10.1371/journal.pone.0051628.

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42

Roach, William, and Markus Plomann. "PACSIN3 overexpression increases adipocyte glucose transport through GLUT1." Biochemical and Biophysical Research Communications 355, no. 3 (April 2007): 745–50. http://dx.doi.org/10.1016/j.bbrc.2007.02.025.

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43

Engevik, Amy C., Izumi Kaji, Meagan M. Postema, James J. Faust, Anne R. Meyer, Janice A. Williams, Gillian N. Fitz, Matthew J. Tyska, Jean M. Wilson, and James R. Goldenring. "Loss of myosin Vb promotes apical bulk endocytosis in neonatal enterocytes." Journal of Cell Biology 218, no. 11 (September 27, 2019): 3647–62. http://dx.doi.org/10.1083/jcb.201902063.

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In patients with inactivating mutations in myosin Vb (Myo5B), enterocytes show large inclusions lined by microvilli. The origin of inclusions in small-intestinal enterocytes in microvillus inclusion disease is currently unclear. We postulated that inclusions in Myo5b KO mouse enterocytes form through invagination of the apical brush border membrane. 70-kD FITC-dextran added apically to Myo5b KO intestinal explants accumulated in intracellular inclusions. Live imaging of Myo5b KO–derived enteroids confirmed the formation of inclusions from the apical membrane. Treatment of intestinal explants and enteroids with Dyngo resulted in accumulation of inclusions at the apical membrane. Inclusions in Myo5b KO enterocytes contained VAMP4 and Pacsin 2 (Syndapin 2). Myo5b;Pacsin 2 double-KO mice showed a significant decrease in inclusion formation. Our results suggest that apical bulk endocytosis in Myo5b KO enterocytes resembles activity-dependent bulk endocytosis, the primary mechanism for synaptic vesicle uptake during intense neuronal stimulation. Thus, apical bulk endocytosis mediates the formation of inclusions in neonatal Myo5b KO enterocytes.
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44

Grimm-Günter, Eva-Maria S., Mark Milbrandt, Barbara Merkl, Mats Paulsson, and Markus Plomann. "PACSIN proteins bind tubulin and promote microtubule assembly." Experimental Cell Research 314, no. 10 (June 2008): 1991–2003. http://dx.doi.org/10.1016/j.yexcr.2008.03.015.

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45

Alet, Claire. "Quand entreprises et ONG se pacsent." Alternatives Économiques 248, no. 6 (June 1, 2006): 42. http://dx.doi.org/10.3917/ae.248.0042.

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46

Han, Gwan Hee, Hanbyoul Cho, Hee Yun, and Jae-Hoon Kim. "PACSIN3 is a novel biomarker for platinum resistance BRCA mutated platinum resistance epithelial ovarian cancer." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e17540-e17540. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e17540.

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e17540 Background: Mutations in breast cancer susceptibility gene type 1 and type 2 (BRCA1 and BRCA2) put women at a higher risk of developing epithelial ovarian cancer (EOC). In individual carrying BRCA1 mutation has about 39-49% of the probability developing EOC in a lifetime. With BRCA2 mutations, the probability of developing EOC is about 11- 18 %. EOC patients with BRCA mutations shows an advanced histological grade compared to patients with BRCA wile type and respond better to platinum therapy, showing better survival. Patients with BRCA mutation shows better response to the platinum therapy, because in the absence of functional BRCA protein, cells fail to repair intra-strand crosslinks formed by DNA cross linking agents such as platinum drugs, leading to apoptotic cell death. However, despite the good response to platinum-based chemotherapy, EOC patients inevitably develop resistance to platinum drugs resulting in disease recurrent and is a major roadblock in a clinical management of cancer that carry BRCA mutation. Therefore, here we investigated the potential novel biomarkers with bioinformatics tools by analyzing an our own RNA sequencing. Methods: RNA sequencing data from 4 platinum sensitive BRCA mutated EOC patients and 4 Platinum resistance BRCA mutated EOC patients were analysed with various bioinformatic tools including Spatial Analysis of Functional Enrichment (SAFE) analysis, and the bioinformatic analysis result was verified with variuos ovarian cancer cell lines and public data. Results: Therefore, here we investigated the potential novel biomarkers with bioinformatics tools by analyzing an our own RNA sequencing data from 4 platinum sensitive BRCA mutated EOC patients and 4 Platinum resistance BRCA mutated EOC patients. The results of our study showed 308 total differentially expressed genes (DEGs) with 138 upregulated genes and 170 downregulated genes. By applying Spatial Analysis of Functional Enrichment (SAFE) analysis, we investigated that G2/M transition of mitotic cell cycle, MAPK cascade, double strand break repair via homologous recombination were the enriched pathways with upregulation of PABPC1, DCAF13, RAD21, PACSIN3 and downregulation of GCG11, HECW2, PSMA1. Their altered expression was verified in ovarian cancer cell lines and public database which showed the significant altered expression of PACSIN3 was observed in ovarian cancer cell lines suggesting as a potential biomarker for EOC treatment. Conclusions: Platinum resistance BRCA mutation EOC is an important issue to overcome the low survival rate for EOC patients. However, until now, there was relatively not much studies in discovring the biomarker or candidate gene of target therapy. Therefore, here we suggest the PACSIN3 as a new candidate gene for target therapy in platinum resistance BRCA mutation EOC.
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47

Han, Gwan Hee, Hanbyoul Cho, Hee Yun, and Jae-Hoon Kim. "PACSIN3 is a novel biomarker for platinum resistance BRCA mutated platinum resistance epithelial ovarian cancer." Journal of Clinical Oncology 40, no. 16_suppl (June 1, 2022): e17540-e17540. http://dx.doi.org/10.1200/jco.2022.40.16_suppl.e17540.

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e17540 Background: Mutations in breast cancer susceptibility gene type 1 and type 2 (BRCA1 and BRCA2) put women at a higher risk of developing epithelial ovarian cancer (EOC). In individual carrying BRCA1 mutation has about 39-49% of the probability developing EOC in a lifetime. With BRCA2 mutations, the probability of developing EOC is about 11- 18 %. EOC patients with BRCA mutations shows an advanced histological grade compared to patients with BRCA wile type and respond better to platinum therapy, showing better survival. Patients with BRCA mutation shows better response to the platinum therapy, because in the absence of functional BRCA protein, cells fail to repair intra-strand crosslinks formed by DNA cross linking agents such as platinum drugs, leading to apoptotic cell death. However, despite the good response to platinum-based chemotherapy, EOC patients inevitably develop resistance to platinum drugs resulting in disease recurrent and is a major roadblock in a clinical management of cancer that carry BRCA mutation. Therefore, here we investigated the potential novel biomarkers with bioinformatics tools by analyzing an our own RNA sequencing. Methods: RNA sequencing data from 4 platinum sensitive BRCA mutated EOC patients and 4 Platinum resistance BRCA mutated EOC patients were analysed with various bioinformatic tools including Spatial Analysis of Functional Enrichment (SAFE) analysis, and the bioinformatic analysis result was verified with variuos ovarian cancer cell lines and public data. Results: Therefore, here we investigated the potential novel biomarkers with bioinformatics tools by analyzing an our own RNA sequencing data from 4 platinum sensitive BRCA mutated EOC patients and 4 Platinum resistance BRCA mutated EOC patients. The results of our study showed 308 total differentially expressed genes (DEGs) with 138 upregulated genes and 170 downregulated genes. By applying Spatial Analysis of Functional Enrichment (SAFE) analysis, we investigated that G2/M transition of mitotic cell cycle, MAPK cascade, double strand break repair via homologous recombination were the enriched pathways with upregulation of PABPC1, DCAF13, RAD21, PACSIN3 and downregulation of GCG11, HECW2, PSMA1. Their altered expression was verified in ovarian cancer cell lines and public database which showed the significant altered expression of PACSIN3 was observed in ovarian cancer cell lines suggesting as a potential biomarker for EOC treatment. Conclusions: Platinum resistance BRCA mutation EOC is an important issue to overcome the low survival rate for EOC patients. However, until now, there was relatively not much studies in discovring the biomarker or candidate gene of target therapy. Therefore, here we suggest the PACSIN3 as a new candidate gene for target therapy in platinum resistance BRCA mutation EOC.
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48

Hansen, C. G., G. Howard, and B. J. Nichols. "Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis." Journal of Cell Science 124, no. 16 (August 1, 2011): 2777–85. http://dx.doi.org/10.1242/jcs.084319.

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49

Halbach, Arndt, Matthias Mörgelin, Maria Baumgarten, Mark Milbrandt, Mats Paulsson, and Markus Plomann. "PACSIN 1 forms tetramers via its N-terminal F-BAR domain." FEBS Journal 274, no. 3 (January 10, 2007): 773–82. http://dx.doi.org/10.1111/j.1742-4658.2006.05622.x.

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50

Edeling, Melissa A., Subramaniam Sanker, Takaki Shima, P. K. Umasankar, Stefan Höning, Hye Y. Kim, Lance A. Davidson, et al. "Structural Requirements for PACSIN/Syndapin Operation during Zebrafish Embryonic Notochord Development." PLoS ONE 4, no. 12 (December 3, 2009): e8150. http://dx.doi.org/10.1371/journal.pone.0008150.

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