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MYL12A  -  myosin, light chain 12A, regulatory, non...

Homo sapiens

Synonyms: Epididymis secretory protein Li 24, HEL-S-24, MLC-2B, MLCB, MRCL3, ...
 
 
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Disease relevance of MRCL3

 

Psychiatry related information on MRCL3

  • The results indicate that the variable Cam_Inst that gathered the impacts of red light camera (RLC) installation on driver decision-making at signalized intersection was significant at 5% level only for the camera approach model of the cross-intersection [6].
  • In addition, patients with RLC showed a significantly lower pain threshold for external mechanical stimuli than those without RLC (Welch's t-test, P < 0.05) [7].
 

High impact information on MRCL3

  • Smooth muscle myosin acts as a molecular motor only if the regulatory light chain (RLC) is phosphorylated [8].
  • Fully functional scallop muscle fibers were prepared such that each myosin molecule contained a terbium-labeled (luminescent donor) RLC on one head and a rhodamine-labeled (acceptor) RLC on the other [9].
  • We have used luminescence resonance energy transfer between regulatory light chains (RLC) to detect structural changes within the dimeric myosin molecule in contracting muscle fibers [9].
  • A key unanswered question in smooth muscle biology is whether phosphorylation of the myosin regulatory light chain (RLC) is sufficient for regulation of contraction, or if thin-filament-based regulatory systems also contribute to this process [10].
  • Following photolysis of caged ATP, cells without calponin that contained a nonphosphorylatable RLC shortened at 30% of the velocity and produced 65% of the isometric force of cells reconstituted with the thiophosphorylated RLC [10].
 

Biological context of MRCL3

  • We have determined the amino acid sequences of the essential light chains (ELC) and regulatory light chains (RLC) of myosin from two species of clam, Mercenaria mercenaria and Macrocallista nimbosa, using protein chemistry methods [11].
  • Thus, the effect of RLC phosphorylation in striated muscle and its ability to regulate the folded-to-extended conformational transition in smooth muscle may be due to a simple reduction of net charge at the N terminus of the light chain [12].
  • Video microscopic observation revealed that cells expressing T18A/S19A RLC showed abnormalities during mitosis in two respects [13].
  • T18A/S19A RLC overexpression resulted in the production of multinucleated cells, suggesting the failure of proper cell division in these cells [13].
  • The other is that separation of chromosomes from the metaphase plate is disrupted in T18A/S19A RLC expressing cells, thus preventing proper transition from metaphase to anaphase [13].
 

Anatomical context of MRCL3

  • We have generated transgenic (Tg) mouse lines of myc-WT (wild type) and myc-E22K mutant of human ventricular RLC and have examined the functional consequences of this FHC mutation in skinned cardiac-muscle preparations [14].
  • The differential expression of the three actin filament-associated proteins--transgelin, vimentin and MRCL3 as well as actin itself--indicates a relevant role of the actin cytoskeleton during pancreatic tumour progression [15].
  • To address this problem, we have produced unphosphorylatable RLC (T18A/S19A RLC) and overexpressed it in COS-7 cells and normal rat kidney cells [13].
  • Prominent stress fibers and focal adhesions were associated with the enhanced RLC phosphorylation [16].
  • The endogenous RLC was removed from skinned rabbit psoas muscle fibers, and replaced with either rat wildtype vRLC or recombinant rat vRLC (G13T, F18L, E22K, and P95A) [17].
 

Associations of MRCL3 with chemical compounds

  • The FHC-mediated structural perturbations in RLC that affect Ca(2+) binding properties of the mutated myocardium are responsible for triggering the abnormal function of the heart that in turn might initiate a hypertrophic process and lead to heart failure [14].
  • On the other hand, deletion of only four N-terminal amino acid residues showed no effect on dephosphorylation of phosphoserine 19 of incorporated RLC [18].
  • The single cysteine (Cys 51) in isolated clam (Mercenaria) RLC was labeled with an indanedione spin label (InVSL) [19].
  • As a practical example, ME distributions were determined with experimental data from muscle fibers labeled with bifunctional rhodamine at known orientations with respect to the myosin regulatory light chain (RLC) [20].
  • Kinetic analysis of contracting fast and slow rabbit muscle fibers in the presence of the tension inhibitor 2,3-butanedione monoxime suggests that regulatory light chain (RLC) phosphorylation up-regulates the flux of weakly attached cross-bridges entering the contractile cycle by increasing the actin-catalyzed release of phosphate from myosin [21].
 

Other interactions of MRCL3

  • Cleavage of either Mercenaria RLC (MRLC) or Macrocallista RLC (VLC) at its 3 Arg yielded four peptides, three of which could not be sequenced directly, due to an N-terminal blocking group and 2 Arg-Gln bonds in these proteins [11].
 

Analytical, diagnostic and therapeutic context of MRCL3

  • These two mutants thus mimicked the behavior of RLC-deficient myosin, with the important difference that the mutant myosins were monodisperse when assayed by sedimentation velocity and electron microscopy [8].
  • Since RLC phosphorylation may be an important determinant of stretch activation in myocardium, we recorded the force responses of skinned myocardium to sudden stretches of 1% of muscle length both before and after treatment with MLCK [22].
  • Baculovirus expression and affinity chromatography were used to isolate heavy meromyosin (HMM) containing one phosphorylated and one dephosphorylated RLC (1-P HMM) [23].
  • The increased immunofluorescence signal from the phosphorylated forms of RLC, together with flow cytometry, provides a clue with which to investigate the mechanisms governing the function of nonmuscle myosins during various cell motile events, including cytokinesis [24].
  • One of the VH/RLC--PhoAs stained one major band on Western blotting of RLC and also stained the cytoplasm of hepatocytes histochemically [3].

References

  1. Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle. Poetter, K., Jiang, H., Hassanzadeh, S., Master, S.R., Chang, A., Dalakas, M.C., Rayment, I., Sellers, J.R., Fananapazir, L., Epstein, N.D. Nat. Genet. (1996) [Pubmed]
  2. Regulation of expressed truncated smooth muscle myosins. Role of the essential light chain and tail length. Trybus, K.M. J. Biol. Chem. (1994) [Pubmed]
  3. Phage library panning against cytosolic fraction of cells using quantitative dot blotting assay: application of selected VH to histochemistry. Nakamura, M., Tsumoto, K., Ishimura, K., Kumagai, I. J. Immunol. Methods (2002) [Pubmed]
  4. Role of lysophosphatidic acid and rho in glioma cell motility. Manning, T.J., Parker, J.C., Sontheimer, H. Cell Motil. Cytoskeleton (2000) [Pubmed]
  5. An evaluation of the performance of XLD, DCA, MLCB, and ABC agars as direct plating media for the isolation of Salmonella enterica from faeces. Nye, K.J., Fallon, D., Frodsham, D., Gee, B., Graham, C., Howe, S., Messer, S., Turner, T., Warren, R.E. J. Clin. Pathol. (2002) [Pubmed]
  6. A before-and-after study of driver stopping propensity at red light camera intersections. Lum, K.M., Wong, Y.D. Accident; analysis and prevention. (2003) [Pubmed]
  7. Relationship between temporomandibular joint (TMJ)-related pain and morphological changes of the TMJ condyle in patients with temporomandibular disorders. Kurita, H., Kojima, Y., Nakatsuka, A., Koike, T., Kobayashi, H., Kurashina, K. Dento maxillo facial radiology. (2004) [Pubmed]
  8. Coupling of ATPase activity and motility in smooth muscle myosin is mediated by the regulatory light chain. Trybus, K.M., Waller, G.S., Chatman, T.A. J. Cell Biol. (1994) [Pubmed]
  9. Coordination of the two heads of myosin during muscle contraction. Lidke, D.S., Thomas, D.D. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  10. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed. Malmqvist, U., Trybus, K.M., Yagi, S., Carmichael, J., Fay, F.S. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  11. Amino acid sequences of myosin essential and regulatory light chains from two clam species: comparison with other molluscan myosin light chains. Barouch, W.W., Breese, K.E., Davidoff, S.A., Leszyk, J., Szent-Györgyi, A.G., Theibert, J.L., Collins, J.H. J. Muscle Res. Cell. Motil. (1991) [Pubmed]
  12. Charge replacement near the phosphorylatable serine of the myosin regulatory light chain mimics aspects of phosphorylation. Sweeney, H.L., Yang, Z., Zhi, G., Stull, J.T., Trybus, K.M. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  13. Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells. Komatsu, S., Yano, T., Shibata, M., Tuft, R.A., Ikebe, M. J. Biol. Chem. (2000) [Pubmed]
  14. The E22K mutation of myosin RLC that causes familial hypertrophic cardiomyopathy increases calcium sensitivity of force and ATPase in transgenic mice. Szczesna-Cordary, D., Guzman, G., Zhao, J., Hernandez, O., Wei, J., Diaz-Perez, Z. J. Cell. Sci. (2005) [Pubmed]
  15. Application of fluorescence difference gel electrophoresis saturation labelling for the analysis of microdissected precursor lesions of pancreatic ductal adenocarcinoma. Sitek, B., Lüttges, J., Marcus, K., Klöppel, G., Schmiegel, W., Meyer, H.E., Hahn, S.A., Stühler, K. Proteomics (2005) [Pubmed]
  16. Myosin phosphatase targeting subunit 1 affects cell migration by regulating myosin phosphorylation and actin assembly. Xia, D., Stull, J.T., Kamm, K.E. Exp. Cell Res. (2005) [Pubmed]
  17. Mechanical defects of muscle fibers with myosin light chain mutants that cause cardiomyopathy. Roopnarine, O. Biophys. J. (2003) [Pubmed]
  18. Role of the N-terminal region of the regulatory light chain in the dephosphorylation of myosin by myosin light chain phosphatase. Ikebe, R., Reardon, S., Mitsui, T., Ikebe, M. J. Biol. Chem. (1999) [Pubmed]
  19. Microsecond rotational dynamics of spin-labeled myosin regulatory light chain induced by relaxation and contraction of scallop muscle. Roopnarine, O., Szent-Györgyi, A.G., Thomas, D.D. Biochemistry (1998) [Pubmed]
  20. A maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes. van der Heide, U.A., Hopkins, S.C., Goldman, Y.E. Biophys. J. (2000) [Pubmed]
  21. Kinetic effects of myosin regulatory light chain phosphorylation on skeletal muscle contraction. Davis, J.S., Satorius, C.L., Epstein, N.D. Biophys. J. (2002) [Pubmed]
  22. Acceleration of Stretch Activation in Murine Myocardium due to Phosphorylation of Myosin Regulatory Light Chain. Stelzer, J.E., Patel, J.R., Moss, R.L. J. Gen. Physiol. (2006) [Pubmed]
  23. Phosphorylation of a single head of smooth muscle myosin activates the whole molecule. Rovner, A.S., Fagnant, P.M., Trybus, K.M. Biochemistry (2006) [Pubmed]
  24. Phosphorylation at threonine-18 in addition to phosphorylation at serine-19 on myosin-II regulatory light chain is a mitosis-specific event. Gerashchenko, B.I., Ueda, K., Hino, M., Hosoya, H. Cytometry. (2002) [Pubmed]
 
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