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Relevant bibliographies by topics / Myosin Regulatory Light chain (RLC20)

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Academic literature on the topic 'Myosin Regulatory Light chain (RLC20)'

Author: Grafiati

Published: 7 September 2023

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Journal articles on the topic "Myosin Regulatory Light chain (RLC20)"

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Artamonov, Mykhaylo V., Swapnil K. Sonkusare, Miranda E. Good, Ko Momotani, Masumi Eto, Brant E. Isakson, Thu H. Le, et al. "RSK2 contributes to myogenic vasoconstriction of resistance arteries by activating smooth muscle myosin and the Na+/H+ exchanger." Science Signaling 11, no. 554 (October 30, 2018): eaar3924. http://dx.doi.org/10.1126/scisignal.aar3924.

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Smooth muscle contraction is triggered when Ca2+/calmodulin-dependent myosin light chain kinase (MLCK) phosphorylates the regulatory light chain of myosin (RLC20). However, blood vessels from Mlck-deficient mouse embryos retain the ability to contract, suggesting the existence of additional regulatory mechanisms. We showed that the p90 ribosomal S6 kinase 2 (RSK2) also phosphorylated RLC20 to promote smooth muscle contractility. Active, phosphorylated RSK2 was present in mouse resistance arteries under normal basal tone, and phosphorylation of RSK2 increased with myogenic vasoconstriction or agonist stimulation. Resistance arteries from Rsk2-deficient mice were dilated and showed reduced myogenic tone and RLC20 phosphorylation. RSK2 phosphorylated Ser19 in RLC in vitro. In addition, RSK2 phosphorylated an activating site in the Na+/H+ exchanger (NHE-1), resulting in cytosolic alkalinization and an increase in intracellular Ca2+ that promotes vasoconstriction. NHE-1 activity increased upon myogenic constriction, and the increase in intracellular pH was suppressed in Rsk2-deficient mice. In pressured arteries, RSK2-dependent activation of NHE-1 was associated with increased intracellular Ca2+ transients, which would be expected to increase MLCK activity, thereby contributing to basal tone and myogenic responses. Accordingly, Rsk2-deficient mice had lower blood pressure than normal littermates. Thus, RSK2 mediates a procontractile signaling pathway that contributes to the regulation of basal vascular tone, myogenic vasoconstriction, and blood pressure and may be a potential therapeutic target in smooth muscle contractility disorders.

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Ihara, Eikichi, Elena Edwards, Meredith A. Borman, David P. Wilson, Michael P. Walsh, and Justin A. MacDonald. "Inhibition of zipper-interacting protein kinase function in smooth muscle by a myosin light chain kinase pseudosubstrate peptide." American Journal of Physiology-Cell Physiology 292, no. 5 (May 2007): C1951—C1959. http://dx.doi.org/10.1152/ajpcell.00434.2006.

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As a regulator of smooth muscle contractility, zipper-interacting protein kinase (ZIPK) appears to phosphorylate the regulatory myosin light chain (RLC20), directly or indirectly, at Ser19 and Thr18 in a Ca2+-independent manner. The calmodulin-binding and autoinhibitory domain of myosin light chain kinase (MLCK) shares similarity to a sequence found in ZIPK. This similarity in sequence prompted an investigation of the SM1 peptide, which is derived from the autoinhibitory region of MLCK, as a potential inhibitor of ZIPK. In vitro studies showed that SM1 is a competitive inhibitor of a constitutively active 32-kDa form of ZIPK with an apparent Ki value of 3.4 μM. Experiments confirmed that the SM1 peptide is also active against full-length ZIPK. In addition, ZIPK autophosphorylation was reduced by SM1. ZIPK activity is independent of calmodulin; however, calmodulin suppressed the in vitro inhibitory potential of SM1, likely as a result of nonspecific binding of the peptide to calmodulin. Treatment of ileal smooth muscle with exogenous ZIPK was accompanied by an increase in RLC20 diphosphorylation, distinguishing between ZIPK [and integrin-linked kinase (ILK)] and MLCK actions. Administration of SM1 suppressed steady-state muscle tension developed by the addition of exogenous ZIPK to Triton-skinned rat ileal muscle strips with or without calmodulin depletion by trifluoperazine. The decrease in contractile force was associated with decreases in both RLC20 mono- and diphosphorylation. In summary, we present the SM1 peptide as a novel inhibitor of ZIPK. We also conclude that the SM1 peptide, which has no effect on ILK, can be used to distinguish between ZIPK and ILK effects in smooth muscle tissues.

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Tsuji, Masayuki, Takao Ojima, and Kiyoyoshi Nishita. "Exchange of DTNB light chain with molluscan myosin regulatory light chain in rabbit myosin." NIPPON SUISAN GAKKAISHI 55, no. 4 (1989): 681–87. http://dx.doi.org/10.2331/suisan.55.681.

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Takashima, Seiji. "Phosphorylation of Myosin Regulatory Light Chain by Myosin Light Chain Kinase, and Muscle Contraction." Circulation Journal 73, no. 2 (2009): 208–13. http://dx.doi.org/10.1253/circj.cj-08-1041.

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Akiyama, K., G. Akopian, P. Jinadasa, T. L. Gluckman, A. Terhakopian, B. Massey, and R. J. Bing. "Myocardial Infarction and Regulatory Myosin Light Chain." Journal of Molecular and Cellular Cardiology 29, no. 10 (October 1997): 2641–52. http://dx.doi.org/10.1006/jmcc.1997.0493.

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Sevrieva, Ivanka R., Birgit Brandmeier, Saraswathi Ponnam, Mathias Gautel, Malcolm Irving, Kenneth S. Campbell, Yin-Biao Sun, and Thomas Kampourakis. "Cardiac myosin regulatory light chain kinase modulates cardiac contractility by phosphorylating both myosin regulatory light chain and troponin I." Journal of Biological Chemistry 295, no. 14 (February 21, 2020): 4398–410. http://dx.doi.org/10.1074/jbc.ra119.011945.

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Heart muscle contractility and performance are controlled by posttranslational modifications of sarcomeric proteins. Although myosin regulatory light chain (RLC) phosphorylation has been studied extensively in vitro and in vivo, the precise role of cardiac myosin light chain kinase (cMLCK), the primary kinase acting upon RLC, in the regulation of cardiomyocyte contractility remains poorly understood. In this study, using recombinantly expressed and purified proteins, various analytical methods, in vitro and in situ kinase assays, and mechanical measurements in isolated ventricular trabeculae, we demonstrate that human cMLCK is not a dedicated kinase for RLC but can phosphorylate other sarcomeric proteins with well-characterized regulatory functions. We show that cMLCK specifically monophosphorylates Ser23 of human cardiac troponin I (cTnI) in isolation and in the trimeric troponin complex in vitro and in situ in the native environment of the muscle myofilament lattice. Moreover, we observed that human cMLCK phosphorylates rodent cTnI to a much smaller extent in vitro and in situ, suggesting species-specific adaptation of cMLCK. Although cMLCK treatment of ventricular trabeculae exchanged with rat or human troponin increased their cross-bridge kinetics, the increase in sensitivity of myofilaments to calcium was significantly blunted by human TnI, suggesting that human cTnI phosphorylation by cMLCK modifies the functional consequences of RLC phosphorylation. We propose that cMLCK-mediated phosphorylation of TnI is functionally significant and represents a critical signaling pathway that coordinates the regulatory states of thick and thin filaments in both physiological and potentially pathophysiological conditions of the heart.

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Kamm, Kristine E., and James T. Stull. "Signaling to Myosin Regulatory Light Chain in Sarcomeres." Journal of Biological Chemistry 286, no. 12 (January 21, 2011): 9941–47. http://dx.doi.org/10.1074/jbc.r110.198697.

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Myosin regulatory light chain (RLC) phosphorylation in skeletal and cardiac muscles modulates Ca2+-dependent troponin regulation of contraction. RLC is phosphorylated by a dedicated Ca2+-dependent myosin light chain kinase in fast skeletal muscle, where biochemical properties of RLC kinase and phosphatase converge to provide a biochemical memory for RLC phosphorylation and post-activation potentiation of force development. The recent identification of cardiac-specific myosin light chain kinase necessary for basal RLC phosphorylation and another potential RLC kinase (zipper-interacting protein kinase) provides opportunities for new approaches to study signaling pathways related to the physiological function of RLC phosphorylation and its importance in cardiac muscle disease.

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Josephson, Matthew P., Laura A. Sikkink, Alan R. Penheiter, Thomas P. Burghardt, and Katalin Ajtai. "Smooth muscle myosin light chain kinase efficiently phosphorylates serine 15 of cardiac myosin regulatory light chain." Biochemical and Biophysical Research Communications 416, no. 3-4 (December 2011): 367–71. http://dx.doi.org/10.1016/j.bbrc.2011.11.044.

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Chaudoir, B. M., P. A. Kowalczyk, and R. L. Chisholm. "Regulatory light chain mutations affect myosin motor function and kinetics." Journal of Cell Science 112, no. 10 (May 15, 1999): 1611–20. http://dx.doi.org/10.1242/jcs.112.10.1611.

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The actin-based motor protein myosin II plays a critical role in many cellular processes in both muscle and non-muscle cells. Targeted disruption of the Dictyostelium regulatory light chain (RLC) caused defects in cytokinesis and multicellular morphogenesis. In contrast, a myosin heavy chain mutant lacking the RLC binding site, and therefore bound RLC, showed normal cytokinesis and development. One interpretation of these apparently contradictory results is that the phenotypic defects in the RLC null mutant results from mislocalization of myosin caused by aggregation of RLC null myosin. To distinguish this from the alternative explanation that the RLC can directly influence myosin activity, we expressed three RLC point mutations (E12T, G18K and N94A) in a Dictyostelium RLC null mutant. The position of these mutations corresponds to the position of mutations that have been shown to result in familial hypertrophic cardiomyopathy in humans. Analysis of purified Dictyostelium myosin showed that while these mutations did not affect binding of the RLC to the MHC, its phosphorylation by myosin light chain kinase or regulation of its activity by phosphorylation, they resulted in decreased myosin function. All three mutants showed impaired cytokinesis in suspension, and one produced defective fruiting bodies with short stalks and decreased spore formation. The abnormal myosin localization seen in the RLC null mutant was restored to wild-type localization by expression of all three RLC mutants. Although two of the mutant myosins had wild-type actin-activated ATPase, they produced in vitro motility rates half that of wild type. N94A myosin showed a fivefold decrease in actin-ATPase and a similar decrease in the rate at which it moved actin in vitro. These results indicate that the RLC can play a direct role in determining the force transmission and kinetic properties of myosin.

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Cummins, C., and P. Anderson. "Regulatory myosin light-chain genes of Caenorhabditis elegans." Molecular and Cellular Biology 8, no. 12 (December 1988): 5339–49. http://dx.doi.org/10.1128/mcb.8.12.5339-5349.1988.

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We have cloned and analyzed the Caenorhabditis elegans regulatory myosin light-chain genes. C. elegans contains two such genes, which we have designated mlc-1 and mlc-2. The two genes are separated by 2.6 kilobases and are divergently transcribed. We determined the complete nucleotide sequences of both mlc-1 and mlc-2. A single, conservative amino acid substitution distinguishes the sequences of the two proteins. The C. elegans proteins are strongly homologous to regulatory myosin light chains of Drosophila melanogaster and vertebrates and weakly homologous to a superfamily of eucaryotic calcium-binding proteins. Both mlc-1 and mlc-2 encode abundant mRNAs. We mapped the 5' termini of these transcripts by using primer extension sequencing of mRNA templates. mlc-1 mRNAs initiate within conserved hexanucleotides at two different positions, located at -28 and -38 relative to the start of translation. The 5' terminus of mlc-2 mRNA is not encoded in the 4.8-kilobase genomic region upstream of mlc-2. Rather, mlc-2 mRNA contains at its 5' end a short, untranslated leader sequence that is identical to the trans-spliced leader sequence of three C. elegans actin genes.

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Dissertations / Theses on the topic "Myosin Regulatory Light chain (RLC20)"

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Willis, Janine Corinth. "Conditions for cardiac muscle myosin regulatory light chain phosphorylation." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/mq64990.pdf.

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Brack, Andrew Stephen. "The orientation change of the myosin regulatory light chain during muscle contraction." Thesis, King's College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.249603.

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Kampourakis, Thomas. "Orientation of the cardiac myosin regulatory light chain determined by polarized fluorescence." Thesis, King's College London (University of London), 2012. https://kclpure.kcl.ac.uk/portal/en/theses/orientation-of-the-cardiac-myosin-regulatory-light-chain-determined-by-polarized-fluorescence(f04760ad-8fc6-4926-b3c7-9c2a1bab7799).html.

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The regulatory light chain (RLC) of myosin is a component of the lever arm of the myosin motor in muscle thick filaments. Phosphorylation of RLC by myosin light chain kinase (MLCK) modulates the force and speed of muscle contraction, but the mechanisms of RLC‐mediated regulation in striated muscles are less well understood than those of Ca2+‐dependent regulation via troponin in the thin filament. To help elucidate the role of RLC in muscle regulation, its orientation in the native environment of cardiac muscle cells was measured. Pairs of cysteine residues were genetically introduced into the N‐ and C‐terminal lobe of the human cardiac RLC. Each pair of cysteines was crosslinked with a bifunctional‐rhodamine (BSR). The pure BSR‐RLC conjugates were exchanged into demembranated trabeculae from rat ventricle, and the orientation of the BSR fluorescence dipole determined by polarized fluorescence. The orientations of the N‐lobe were similar to those determined from chicken gizzard RLC probes exchanged into skeletal muscle fibers indicating a conserved domain orientation. The orientation of the RLC C ‐ lobe was similar in relaxation, active isometric contraction and rigor, suggesting that either the orientation of the RLC is relatively insensitive to strong binding of myosin heads to actin, or that only a small fraction of myosin heads are strongly bound to the thin filament in both active isometric contraction and rigor. Bending between the two RLC lobes occurs in ‐ situ and may have a functional significance in cardiac muscle contraction and regulation. Expressed and purified catalytic subunit of human cardiac MLCK efficiently mono ‐ phosphorylates cardiac RLC on serine 15 in a calcium/calmodulin dependent manner. Exchange of in ‐ vitro phosphorylated BSR‐RLCs into demembranated trabeculae to replace 10‐15% of native RLC showed that the orientation of phosphorylated RLC C ‐ lobe is similar to that of unphosphorylated RLCs.

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Tohtong, Rutaiwan. "Analysis of the in vivo role of myosin regulatory light chain phosphorylation /." The Ohio State University, 1994. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487854314873463.

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Toepfer, Christopher. "The role of myosin regulatory light chain phosphorylation in cardiac health and disease." Thesis, Imperial College London, 2015. http://hdl.handle.net/10044/1/30846.

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In this thesis we examined the effect of myosin associated regulatory light chain (RLC) phosphorylation level on cardiac muscle, ensembles and single molecules. We measured the ability of RLC phosphorylation change in muscle to alter force, power and unloaded shortening. The ATPase rate of full length cardiac myosin was determined with a novel protocol using gelsolin capped actin, which allowed novel measurements of myosin ATPase with full length (filamentous) myosin in low ionic strength. Actin gliding assays determined the effects of RLC phosphorylation level on actin gliding velocities under high and negligible load. The lifetime of strongly bound actomyosin states and the displacement of single myosin molecules were examined using an optical trapping three bead assay. A quantitative Phos-tag SDS-PAGE protocol was used to assess RLC phosphorylation level in inherited (mutation) and acquired (infarct and heart failure) human and rat diseases. Cardiac disorders in human and rat left ventricular myocardium correlated with increased RLC phosphorylation. RLC phosphorylation alters the ability of muscle to produce force, power and maximal unloaded shortening. Increased RLC phosphorylation accelerated the ATPase rate of cardiac myosin; reduced the lifetime of strongly bound actomyosin states and increased the displacement of actin by myosin. This data correlated with an increased ability of myosin with phosphorylated RLCs to translocate actin, under high and low load in the actin gliding assay. Cardiac myosin with raised RLC phosphorylation can produce more force and power during shortening due to changes in ATPase cycle, lifetime of the strongly bound states and power stroke size under load. Therefore myosin can perform work on actin faster and produce a longer actin displacement with each cycle. Thus proving that RLC phosphorylation level alteration impacts systolic myocardial performance in human health and disease by altering both myosin mechanics and kinetics.

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de, Freitas Fatima Pestana. "The Importance of Fast Skeletal Regulatory Light Chain in Muscle Contraction." Scholarly Repository, 2008. http://scholarlyrepository.miami.edu/oa_theses/97.

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The aim of this project was to produce and study a murine homozygous knock-in model containing a fast skeletal regulatory light chain (RLC) containing a Asp49toAla point mutation. The D49A mutation is in the functional calcium binding loop of RLC, which is believed to modulate muscle contraction in striated muscle. To introduce the mutation, a reversible knock-out/knock-in system was employed. The Cre/Lox-P strategy was used to conditionally knock-in the RLC D49A mutation. The generation of the knock-in mouse was attempted with two different breeding strategies consisting of two Cre mouse lines with differential expression patterns during development. The proposed animal was never produced because the RLC knock-out recombination event introduced a splicing error resulting in a stop codon in intron 2. Extensive DNA, RNA and protein analysis as well as histological, gross morphology and muscle physiology studies obtained from the animals of the two breeding strategies lead to the identification of the splicing error. Evidence for this outcome is presented. A recommendation for a different strategy in future studies is included.

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Patel, Sejal. "Myosin regulatory light chain phosphorylation and its role in active mechanics and force generation of the heart." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p1462361.

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Thesis (M.S.)--University of California, San Diego, 2009.
Title from first page of PDF file (viewed May 4, 2009). Available via ProQuest Digital Dissertations. Includes bibliographical references (p. 43-48).

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Ip, Kelvin. "Mechanical integrity of myosin thick filaments of airway smooth muscle in vitro: effects of phosphoryation of the regulatory light chain." Thesis, University of British Columbia, 2008. http://hdl.handle.net/2429/4131.

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Background and aims: It is known that smooth muscle possesses substantial mechanical plasticity in that it is able to adapt to large changes in length without compromising its ability to generate force. It is believed that structural malleability of the contractile apparatus underlies this plasticity. There is strong evidence suggesting that myosin thick filaments of the muscle are relatively labile and their length in vivo is determined by the equilibrium between monomeric and filamentous myosin. The equilibrium in turn is governed by the state of phosphorylation of the 20-kD regulatory myosin light chain (MLC20, or RLC). It is known that phosphorylation of the myosin light chain favors formation of the filaments; it is not known how the light chain phosphorylation affects the lability of the filaments. The major aim of this thesis was to measure the mechanical integrity of the filaments formed from purified myosin molecules from bovine airway smooth muscle, and to determine whether the integrity was influenced by phosphorylation of the myosin light chain. Methods: Myosin was purified from bovine trachealis to form filaments, in ATP containing zero-calcium solution during a slow dialysis that gradually reduced the ionic strength. Sufficient myosin light chain kinase and phosphatase, as well as calmodulin, were retained after the myosin purification and this enabled phosphorylation of RLC within 20-40 s after addition of calcium to the filament suspension. The phosphorylated and non-phosphorylated filaments were then partially disassembled by ultrasonification. The extent of filament disintegration was visualized and quantified by atomic force microscopy. Results: RLC phosphorylation reduced the diameter of the filaments and rendered the filaments more resistant to ultrasonic agitation. Electron microscopy revealed a similar reduction in filament diameter in intact smooth muscle when the cells were activated. Conclusion: Our results suggest that RLC phosphorylation is a key regulatory step in modifying the structural properties of myosin filaments in smooth muscle, where formation and dissolution of the filaments are required in the cells’ adaptation to different cell length.

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9

Saramago, Joana Filipa Silva. "Phospho-regulation of Myosin Regulatory Light Chain in Caenorhabditis elegans embryos during cytokinesis." Master's thesis, 2014. https://repositorio-aberto.up.pt/handle/10216/80077.

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Saramago, Joana Filipa Silva. "Phospho-regulation of Myosin Regulatory Light Chain in Caenorhabditis elegans embryos during cytokinesis." Dissertação, 2014. https://repositorio-aberto.up.pt/handle/10216/80077.

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Book chapters on the topic "Myosin Regulatory Light chain (RLC20)"

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Doevendans, Pieter A., Ronald Bronsaer, Pilar Ruiz-Lozano, Jan Melle van Dantzig, and Marc van Bilsen. "Ventricular Expression of the Atrial Regulatory Myosin Light Chain Gene." In Developments in Cardiovascular Medicine, 99–116. Dordrecht: Springer Netherlands, 1999. http://dx.doi.org/10.1007/978-94-015-9321-2_10.

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Schaub, M. C., A. Jauch, P. Huber, U. T. Brunner, and T. Wallimann. "Shape Changes in Myosin Induced by the Regulatory Light Chain Subunits." In Springer Series in Biophysics, 163–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-73925-5_31.

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Nabeshima, Yo-ichi, Taichi Uetsuki, Thorn Komiya, Yoko Nabeshima, and Atsuko Fujisawa-Sehara. "Regulatory elements involved in chicken myosin alkali light chain gene expression." In The Dynamic State of Muscle Fibers, edited by Dirk Pette, 33–44. Berlin, Boston: De Gruyter, 1990. http://dx.doi.org/10.1515/9783110884784-006.

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Muthu, Priya, Wenrui Huang, Katarzyna Kazmierczak, and Danuta Szczesna-Cordary. "Functional Consequences of Mutations in the Myosin Regulatory Light Chain Associated with Hypertrophic Cardiomyopathy." In Cardiomyopathies - From Basic Research to Clinical Management. InTech, 2012. http://dx.doi.org/10.5772/29012.

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Conference papers on the topic "Myosin Regulatory Light chain (RLC20)"

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Zheng, Z., Y. Wang, X. Wang, and S. Wu. "Angiotensin II Potentiation Contributes to Inter-Endothelial Cell Gap Formation in Pulmonary Microvascular Endothelial Cells Through Regulatory Myosin Light Chain 2 Phosphorylation." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4386.

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Reports on the topic "Myosin Regulatory Light chain (RLC20)"

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Sadot, Einat, Christopher Staiger, and Mohamad Abu-Abied. Studies of Novel Cytoskeletal Regulatory Proteins that are Involved in Abiotic Stress Signaling. United States Department of Agriculture, September 2011. http://dx.doi.org/10.32747/2011.7592652.bard.

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In the original proposal we planned to focus on two proteins related to the actin cytoskeleton: TCH2, a touch-induced calmodulin-like protein which was found by us to interact with the IQ domain of myosin VIII, ATM1; and ERD10, a dehydrin which was found to associate with actin filaments. As reported previously, no other dehydrins were found to interact with actin filaments. In addition so far we were unsuccessful in confirming the interaction of TCH2 with myosin VIII using other methods. In addition, no other myosin light chain candidates were found in a yeast two hybrid survey. Nevertheless we have made a significant progress in our studies of the role of myosins in plant cells. Plant myosins have been implicated in various cellular activities, such as cytoplasmic streaming (1, 2), plasmodesmata function (3-5), organelle movement (6-10), cytokinesis (4, 11, 12), endocytosis (4, 5, 13-15) and targeted RNA transport (16). Plant myosins belong to two main groups of unconventional myosins: myosin XI and myosin VIII, both closely related to myosin V (17-19). The Arabidopsis myosin family contains 17 members: 13 myosin XI and four myosin VIII (19, 20). The data obtained from our research of myosins was published in two papers acknowledging BARD funding. To address whether specific myosins are involved with the motility of specific organelles, we cloned the cDNAs from neck to tail of all 17 Arabidopsis myosins. These were fused to GFP and used as dominant negative mutants that interact with their cargo but are unable to walk along actin filaments. Therefore arrested organelle movement in the presence of such a construct shows that a particular myosin is involved with the movement of that particular organelle. While no mutually exclusive connections between specific myosins and organelles were found, based on overexpression of dominant negative tail constructs, a group of six myosins (XIC, XIE, XIK, XI-I, MYA1 and MYA2) were found to be more important for the motility of Golgi bodies and mitochondria in Nicotiana benthamiana and Nicotiana tabacum (8). Further deep and thorough analysis of myosin XIK revealed a potential regulation by head and tail interaction (Avisar et al., 2011). A similar regulatory mechanism has been reported for animal myosin V and VIIa (21, 22). In was shown that myosin V in the inhibited state is in a folded conformation such that the tail domain interacts with the head domain, inhibiting its ATPase and actinbinding activities. Cargo binding, high Ca2+, and/or phosphorylation may reduce the interaction between the head and tail domains, thus restoring its activity (23). Our collaborative work focuses on the characterization of the head tail interaction of myosin XIK. For this purpose the Israeli group built yeast expression vectors encoding the myosin XIK head. In addition, GST fusions of the wild-type tail as well as a tail mutated in the amino acids that mediate head to tail interaction. These were sent to the US group who is working on the isolation of recombinant proteins and performing the in vitro assays. While stress signals involve changes in Ca2+ levels in plants cells, the cytoplasmic streaming is sensitive to Ca2+. Therefore plant myosin activity is possibly regulated by stress. This finding is directly related to the goal of the original proposal.

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