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      Myosin light chains: Teaching old dogs new tricks

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          Abstract

          The myosin holoenzyme is a multimeric protein complex consisting of heavy chains and light chains. Myosin light chains are calmodulin family members which are crucially involved in the mechanoenzymatic function of the myosin holoenzyme. This review examines the diversity of light chains within the myosin superfamily, discusses interactions between the light chain and the myosin heavy chain as well as regulatory and structural functions of the light chain as a subunit of the myosin holoenzyme. It covers aspects of the myosin light chain in the localization of the myosin holoenzyme, protein-protein interactions and light chain binding to non-myosin binding partners. Finally, this review challenges the dogma that myosin regulatory and essential light chain exclusively associate with conventional myosin heavy chains while unconventional myosin heavy chains usually associate with calmodulin.

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          Three-dimensional structure of myosin subfragment-1: a molecular motor.

          Rachel M Holden, I Rayment, Wojciech R Rypniewski … (1993)
          Directed movement is a characteristic of many living organisms and occurs as a result of the transformation of chemical energy into mechanical energy. Myosin is one of three families of molecular motors that are responsible for cellular motility. The three-dimensional structure of the head portion of myosin, or subfragment-1, which contains both the actin and nucleotide binding sites, is described. This structure of a molecular motor was determined by single crystal x-ray diffraction. The data provide a structural framework for understanding the molecular basis of motility.
          Article 0 comments Cited 143 times – based on 0 reviews     Review now
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            Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin.

            M. A. Schumacher, A Rivard, H Bächinger … (2001)
            Small-conductance Ca2+-activated K+ channels (SK channels) are independent of voltage and gated solely by intracellular Ca2+. These membrane channels are heteromeric complexes that comprise pore-forming alpha-subunits and the Ca2+-binding protein calmodulin (CaM). CaM binds to the SK channel through the CaM-binding domain (CaMBD), which is located in an intracellular region of the alpha-subunit immediately carboxy-terminal to the pore. Channel opening is triggered when Ca2+ binds the EF hands in the N-lobe of CaM. Here we report the 1.60 A crystal structure of the SK channel CaMBD/Ca2+/CaM complex. The CaMBD forms an elongated dimer with a CaM molecule bound at each end; each CaM wraps around three alpha-helices, two from one CaMBD subunit and one from the other. As only the CaM N-lobe has bound Ca2+, the structure provides a view of both calcium-dependent and -independent CaM/protein interactions. Together with biochemical data, the structure suggests a possible gating mechanism for the SK channel.
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              Reassessing the role and dynamics of nonmuscle myosin II during furrow formation in early Drosophila embryos.

              Christine Field, Roger E. Karess, Kayla Sisson … (2004)
              The early Drosophila embryo undergoes two distinct membrane invagination events believed to be mechanistically related to cytokinesis: metaphase furrow formation and cellularization. Both involve actin cytoskeleton rearrangements, and both have myosin II at or near the forming furrow. Actin and myosin are thought to provide the force driving membrane invagination; however, membrane addition is also important. We have examined the role of myosin during these events in living embryos, with a fully functional myosin regulatory light-chain-GFP chimera. We find that furrow invagination during metaphase and cellularization occurs even when myosin activity has been experimentally perturbed. In contrast, the basal closure of the cellularization furrows and the first cytokinesis after cellularization are highly dependent on myosin. Strikingly, when ingression of the cellularization furrow is experimentally inhibited by colchicine treatment, basal closure still occurs at the appropriate time, suggesting that it is regulated independently of earlier cellularization events. We have also identified a previously unrecognized reservoir of particulate myosin that is recruited basally into the invaginating furrow in a microfilament-independent and microtubule-dependent manner. We suggest that cellularization can be divided into two distinct processes: furrow ingression, driven by microtubule mediated vesicle delivery, and basal closure, which is mediated by actin/myosin based constriction.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Bioarchitecture
                Journal ID (iso-abbrev): Bioarchitecture
                Journal ID (pmc): KBIA
                Title: Bioarchitecture
                Publisher: Taylor & Francis
                ISSN (Print): 1949-0992
                ISSN (Electronic): 1949-100X
                Publication date Collection: 2014
                Publication date (Electronic): 9 July 2015
                Publication date PMC-release: 9 July 2015
                Volume: 4
                Issue: 6
                Pages: 169-188
                Affiliations
                Laboratory of Molecular Physiology; National Heart, Lung, and Blood Institute; National Institutes of Health ; Bethesda, MD USA
                Author notes
                [* ]Correspondence to: James R Sellers; Email: sellersj@ 123456nhlbi.nih.gov
                Article
                Publisher ID: 1054092
                DOI: 10.1080/19490992.2015.1054092
                PMC ID: 4914028
                PubMed ID: 26155737
                SO-VID: dc83ca93-9106-4fcf-95bb-3ab7befb0901
                Copyright © © 2015 The Author(s). Published by Taylor & Francis
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License ( http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 14 April 2015
                Date revision received : 11 May 2015
                Date accepted : 14 May 2015
                Page count
                Figures: 4, Tables: 3, References: 221, Pages: 20
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: actin,calmodulin,cytoskeleton,essential light chain,live cell imaging,myosin,regulatory light chain
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: actin, calmodulin, cytoskeleton, essential light chain, live cell imaging, myosin, regulatory light chain

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