Relevant bibliographies by topics / Mucolipin

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  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Mucolipin'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Mucolipin"

1

Puertollano, Rosa, and Kirill Kiselyov. "TRPMLs: in sickness and in health." American Journal of Physiology-Renal Physiology 296, no. 6 (June 2009): F1245—F1254. http://dx.doi.org/10.1152/ajprenal.90522.2008.

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TRPML1, TRPML2 and TRPML3 belong to the mucolipin family of the TRP superfamily of ion channels. The founding member of this family, TRPML1, was cloned during the search for the genetic determinants of the lysosomal storage disease mucolipidosis type IV (MLIV). Mucolipins are predominantly expressed within the endocytic pathway, where they appear to regulate membrane traffic and/or degradation. The physiology of mucolipins raises some of the most interesting questions of modern cell biology. Their traffic and localization is a multistep process involving a system of adaptor proteins, while their ion channel activity possibly exemplifies the rare cases of regulation of endocytic traffic and hydrolysis by ion channels. Finally, dysregulation of mucolipins results in cell death leading to neurodegenerative phenotypes of MLIV and of the varitint-waddler mouse model of familial deafness. The present review discusses current knowledge and questions regarding this novel family of disease-relevant ion channels with a specific focus on mucolipin regulation and their role in membrane traffic and cell death. Since mucolipins are ubiquitously expressed, this review may be useful for a wide audience of basic biologists and clinicians.
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Vergarajauregui, Silvia, Ross Oberdick, Kirill Kiselyov, and Rosa Puertollano. "Mucolipin 1 channel activity is regulated by protein kinase A-mediated phosphorylation." Biochemical Journal 410, no. 2 (February 12, 2008): 417–25. http://dx.doi.org/10.1042/bj20070713.

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Mucolipins constitute a family of cation channels with homology with the transient receptor potential family. Mutations in MCOLN1 (mucolipin 1) have been linked to mucolipidosis type IV, a recessive lysosomal storage disease characterized by severe neurological and ophthalmologic abnormalities. At present, little is known about the mechanisms that regulate MCOLN1 activity. In the present paper, we addressed whether MCOLN1 activity is regulated by phosphorylation. We identified two PKA (protein kinase A) consensus motifs in the C-terminal tail of MCOLN1, containing Ser557 and Ser559. Ser557 was the principal phosphorylation site, as mutation of this residue to alanine caused a greater than 75% reduction in the total levels of phosphorylated MCOLN1 C-terminal tail. Activation of PKA with forskolin promoted MCOLN1 phosphorylation, both in vitro and in vivo. In contrast, addition of the PKA inhibitor H89 abolished MCOLN1 phosphorylation. We also found that PKA-mediated phosphorylation regulates MCOLN1 channel activity. Forskolin treatment decreased MCOLN1 channel activity, whereas treatment with H89 increased MCOLN1 channel activity. The stimulatory effect of H89 on MCOLN1 function was not observed when Ser557 and Ser559 were mutated to alanine residues, indicating that these two residues are essential for PKA-mediated negative regulation of MCOLN1. This paper presents the first example of regulation of a member of the mucolipin family by phosphorylation.
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Lima, W. C., F. Leuba, T. Soldati, and P. Cosson. "Mucolipin controls lysosome exocytosis in Dictyostelium." Journal of Cell Science 125, no. 9 (February 22, 2012): 2315–22. http://dx.doi.org/10.1242/jcs.100362.

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Curcio-Morelli, Cyntia, Peng Zhang, Bhuvarahamurthy Venugopal, Florie A. Charles, Marsha F. Browning, Horacio F. Cantiello, and Susan A. Slaugenhaupt. "Functional multimerization of mucolipin channel proteins." Journal of Cellular Physiology 222, no. 2 (February 2010): 328–35. http://dx.doi.org/10.1002/jcp.21956.

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Zufferey, Madeleine, and Cedric Blanc. "The RA11 and RA12 antibodies recognize a peptide of the D. discoideum Mucolipin protein by western blot." Antibody Reports 3, no. 1 (February 6, 2020): e127. http://dx.doi.org/10.24450/journals/abrep.2020.e127.

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Bach, Gideon. "Mucolipin 1: endocytosis and cation channel—a review." Pflügers Archiv - European Journal of Physiology 451, no. 1 (November 27, 2004): 313–17. http://dx.doi.org/10.1007/s00424-004-1361-7.

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Al-Alawi, Badriya, Beena Harikrishna, Khalid Al-Thihli, Sana Al Zuhabi, Anuradha Ganesh, Zainab Al Hashami, Zeyana Al Dhamhmani, Razan Zadjali, Nafila B. Al Riyami, and Fahad Zadjali. "Mucolipidosis Type IV in Omani Families with a Novel MCOLN1 Mutation: Search for Evidence of Founder Effect." Genes 13, no. 2 (January 28, 2022): 248. http://dx.doi.org/10.3390/genes13020248.

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Mucolipidosis Type IV (MLIV) is caused by a deficiency of the mucolipin cation channel encoded by Mucolipin TRP Cation Channel 1 gene (MCOLN1). It is a slowly progressive neurodevelopmental and neurodegenerative disorder causing severe psychomotor developmental delay and progressive visual impairment, which is often misdiagnosed as cerebral palsy. We describe six patients with MLIV from two Omani families with a novel c.237+5G>A mutation in the MCOLN1 gene predicted to affect mRNA splicing. Mutation screening with a high-resolution melting (HRM) assay in a large population sample did not detect this mutation in control subjects. This report highlights the importance of considering MLIV in the differential diagnosis of patients in a pediatric age group with cerebral palsy-like presentation. Although the same rare mutation was seen in two apparently unrelated families, this was not seen in the sample screened from the general population. The HRM assay provides a cost-effective assay for population screening for the c.237+5G>A mutation.
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Thompson, Eric G., Lara Schaheen, Hope Dang, and Hanna Fares. "Lysosomal trafficking functions of mucolipin-1 in murine macrophages." BMC Cell Biology 8, no. 1 (2007): 54. http://dx.doi.org/10.1186/1471-2121-8-54.

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Curcio-Morelli, Cyntia, Florie A. Charles, Matthew C. Micsenyi, Yi Cao, Bhuvarahamurthy Venugopal, Marsha F. Browning, Kostantin Dobrenis, Susan L. Cotman, Steven U. Walkley, and Susan A. Slaugenhaupt. "Macroautophagy is defective in mucolipin-1-deficient mouse neurons." Neurobiology of Disease 40, no. 2 (November 2010): 370–77. http://dx.doi.org/10.1016/j.nbd.2010.06.010.

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Bach, Gideon, David A. Zeevi, Ayala Frumkin, and Aviram Kogot-Levin. "Mucolipidosis type IV and the mucolipins." Biochemical Society Transactions 38, no. 6 (November 24, 2010): 1432–35. http://dx.doi.org/10.1042/bst0381432.

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MLIV (mucolipidosis type IV) is a neurodegenerative lysosomal storage disorder caused by mutations in MCOLN1, a gene that encodes TRPML1 (mucolipin-1), a member of the TRPML (transient receptor potential mucolipin) cation channels. Two additional homologues are TRPML2 and TRPML3 comprising the TRPML subgroup in the TRP superfamily. The three proteins play apparently key roles along the endocytosis process, and thus their cellular localization varies among the different group members. Thus TRPML1 is localized exclusively to late endosomes and lysosomes, TRPML2 is primarily located in the recycling clathrin-independent GPI (glycosylphosphatidylinositol)-anchored proteins and early endosomes, and TRPML3 is primarily located in early endosomes. Apparently, all three proteins' main physiological function underlies Ca2+ channelling, regulating the endocytosis process. Recent findings also indicate that the three TRPML proteins form heteromeric complexes at least in some of their cellular content. The physiological role of these complexes in lysosomal function remains to be elucidated, as well as their effect on the pathophysiology of MLIV. Another open question is whether any one of the TRPMLs bears additional function in channel activity
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Dissertations / Theses on the topic "Mucolipin"

1

Thompson, Eric, Lara Schaheen, Hope Dang, and Hanna Fares. "Lysosomal trafficking functions of mucolipin-1 in murine macrophages." BioMed Central, 2007. http://hdl.handle.net/10150/610354.

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BACKGROUND:Mucolipidosis Type IV is currently characterized as a lysosomal storage disorder with defects that include corneal clouding, achlorhydria and psychomotor retardation. MCOLN1, the gene responsible for this disease, encodes the protein mucolipin-1 that belongs to the "Transient Receptor Potential" family of proteins and has been shown to function as a non-selective cation channel whose activity is modulated by pH. Two cell biological defects that have been described in MLIV fibroblasts are a hyperacidification of lysosomes and a delay in the exit of lipids from lysosomes.RESULTS:We show that mucolipin-1 localizes to lysosomal compartments in RAW264.7 mouse macrophages that show subcompartmental accumulations of endocytosed molecules. Using stable RNAi clones, we show that mucolipin-1 is required for the exit of lipids from these compartments, for the transport of endocytosed molecules to terminal lysosomes, and for the transport of the Major Histocompatibility Complex II to the plasma membrane.CONCLUSION:Mucolipin-1 functions in the efficient exit of molecules, destined for various cellular organelles, from lysosomal compartments.
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Durns, Tyler Adam. "Identifying Mucolipin Interactors Using the Split-Ubiquitin Yeast Two-Hybrid System." Thesis, The University of Arizona, 2011. http://hdl.handle.net/10150/144315.

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RIGAMONTI, MARCO. "HYPOTONIC STRESS-INDUCED CALCIUM SIGNALLING IN S. CEREVISIAE INVOLVES A NEW FUNGAL SPECIFIC FAMILY OF TRP-LIKE TRANSPORTERS, HOMOLOGOUS TO HUMAN MUCOLIPIN AND POLYCYSTIC KIDNEY DISEASE RELATED (PKD2) CALCIUM CHANNELS." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/71811.

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Studi presenti in letteratura hanno dimostrato che nel lievito S.cerevisiae lo stress generato dallo shock ipotonico induce un aumento transiente della [Ca2+]i. Dai nostri studi risulta che lo shock ipotonico è mediato, in cellule cresciute in terreno ricco, da due componenti cineticamente distinte, una molto rapida (circa 5 secondi), leggermente inibita da calcio e dipendente dal calcio extracellulare, e l’altra più lenta (10-20 sec.), fortemente sensibile alla presenza di calcio nell’ambiente esterno, al punto da non essere rilevabile anche a concentrazioni extracellulari di 1 µM. Mentre la prima risposta sembra essere mediata da un trasportatore localizzato sulla membrana plasmaticala seconda è chiaramente dipendente da un rilascio dagli store intracellulari. Alcuni dati presenti in letteratura sui geni regolati dal calcio ci hanno suggerito di studiare il ruolo nella risposta a shock ipotonico di due geni omologhi, di cui il primo è stata proposto come codificante per un putativo canale per ioni simile ai canali TRP di mammifero: YOR365C e FLC2. Flc2 è localizzata sulle membrane plasmatica, di Golgi ed ER ed è stato proposto come putativo trasportatore di flavine assieme ai suoi omologhi Flc1 e Flc3. Tuttavia Flc2 era già stato precedentemente identificato come un omologo del canale del calcio pkd2 di S. pombe. Effettivamente in base a nostri allineamenti è risultato evidente come Flc2 appartenga a una sottofamiglia di canali TRP-like tipica dei funghi, a cui appartengono anche le mucolipine umane e le proteine spray fungine, ma non le proteine Pkd2. Solo la mancanza di FLC2 abbatteva completamente il rilascio di calcio dagli store intracellulari in carenza di calcio extracellulare, indicando che questi geni, pur appartenenti alla stessa famiglia, svolgono funzioni molto diverse. Per caratterizzare in modo efficace i flussi di calcio dovuti allo shock ipotonico abbiamo calcolato la velocità iniziale di incremento della [Ca2+]i (v0) al variare della concentrazione di calcio extracellulare. Nel ceppo selvatico i dati in nostro possesso non potevano essere interpolati da nessuna equazione di Hill, a causa di una componente additiva presente a concentrazioni submicromolari di calcio extracellulare, mentre prendendo in considerazione i dati rilevati a concentrazioni di calcio superiori a1µM possiamo osservare una perfetta Michaelis-Menten caratterizzata da una KM di 1 µM. A concentrazioni di calcio superiori a 1 µM invece la v0 subisce una forte inibizione dovuta al calcio stesso,con una IC50 di 20 µM. Al contrario i dati delle v0 calcolati nel ceppo flc2∆ sono interpolati da una curva di Hill anche a concentrazioni submicromolari di calcio,in quanto non si rileva alcuna componente additiva (dovuta probabilmente al rilascio di calcio dall’ER controllato da Flc2) a basse concentrazioni di calcio, né d’altra parte si osserva l’inibizione ad alte concentrazioni. Anche in questo caso la k è di circa 1 µM e la curva mostra un numero di cooperatività di 3. Questi dati ci portano ad affermare che il flusso di calcio a seguito di uno shock ipotonico è caratterizzato dall’attività di due diversi complessi: uno localizzato sull’ER, attivo solo quando non è disponibile calcio extracellulare e regolato da Flc2, che ha probabilmente funzione di trasporto o di attivazione del complesso; l’altro sulla membrana plasmatica, attivo solo quando è presente calcio nell’ambiente extracellulare a concentrazioni micromolari. La peculiarità di quest’ultimo complesso è che, alla luce della scomparsa dell’inibizione ad alte concentrazioni di calcio osservata nel ceppo flc2∆, anch’esso sembra coinvolgere l’attività della proteina Flc2, che è probabilmente la sub unità regolatoria sensibile al calcio del trasportatore in questione.
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Lepow, Talya Shanna. "IDENTIFICATION OF INTERACTORS OF MUCOLIPINS." Thesis, The University of Arizona, 2009. http://hdl.handle.net/10150/192531.

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Book chapters on the topic "Mucolipin"

1

García-Añoveros, Jaime, and Teerawat Wiwatpanit. "TRPML2 and Mucolipin Evolution." In Handbook of Experimental Pharmacology, 647–58. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-54215-2_25.

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Zhang, Fan, and Pin-Lan Li. "Lysosomal Transient Receptor Potential Mucolipin (TRPML) Channels in Vascular Regulation and Diseases." In Vascular Ion Channels in Physiology and Disease, 215–29. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-29635-7_10.

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Gewies, Andreas, Jürgen Ruland, Alexey Kotlyarov, Matthias Gaestel, Shiri Procaccia, Rony Seger, Shin Yasuda, et al. "Mucolipins, TRPML1-3." In Encyclopedia of Signaling Molecules, 1142. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100866.

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4

Flores, Emma N., and Jaime García-Añoveros. "TRPML2 and the Evolution of Mucolipins." In Transient Receptor Potential Channels, 221–28. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0265-3_12.

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"Mucolipins, TRPML1-3." In Encyclopedia of Signaling Molecules, 3269. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_102429.

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