The myosin superfamily at a glance

Department of Biochemistry, Stanford University, Stanford, CA 94305, USA.
Journal of Cell Science (Impact Factor: 5.43). 04/2012; 125(Pt 7):1627-32. DOI: 10.1242/jcs.094300
Source: PubMed
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    • "Myosin VI is an ATP hydrolysis coupled motor protein involved in many cellular functions including endocytosis, protein secretion and the maintenance of both the Golgi morphology and stereocilia [1]. It is a unique myosin in that it moves to the minus end of an actin filament [2], while all other myosins move to the plus end [3]. Recently, we proposed that myosin VI moves using three types of steps: large and small forward steps (minus end directed), and backward steps (plus end directed) [4] [5] [6]. "
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    ABSTRACT: Myosin VI is a processive myosin that has a unique stepping motion, which includes three kinds of steps: a large forward step, a small forward step and a backward step. Recently, we proposed the parallel lever arms model to explain the adjacent binding state, which is necessary for the unique motion. In this model, both lever arms are directed the same direction. However, experimental evidence has not refuted the possibility that the adjacent binding state emerges from myosin VI folding its lever arm extension (LAE). To clarify this issue, we constructed a myosin VI/V chimera that replaces the myosin VI LAE with the IQ3-6 domains of the myosin V lever arm, which cannot fold, and performed single molecule imaging. Our chimera showed the same stepping patterns as myosin VI, indicating the LAE is not responsible for the adjacent binding state.
    BIOPHYSICS 01/2015; 11. DOI:10.2142/biophysics.11.47
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    • "These newly discovered myosin-like molecules are referred to as unconventional myosins. There are about 20 classes of these molecules (Krendel and Mooseker, 2005; Hartman and Spudich, 2012). Redowicz and coworker (Karolczak et al., 2014) review the distribution and roles of one of these unconventional myosins, myosin VIA, in healthy and in diseased striated muscle cells. "
    The Anatomical Record Advances in Integrative Anatomy and Evolutionary Biology 09/2014; 297(9). DOI:10.1002/ar.22986 · 1.54 Impact Factor
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    • "Myosin Superfamily M yosins are actin-dependent molecular motors that utilize the energy of ATP hydrolysis to generate force. The many functions of myosins include cell contractility, cell signaling, endocytosis, vesicle trafficking and protein/ RNA localization [Krendel and Mooseker, 2005; Woolner and Bement, 2009; Hartman and Spudich, 2012]. All myosins share certain structural and functional features, particularly the presence of an actin-binding head domain, which is also responsible for myosin ATPase activity. "
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    ABSTRACT: The actin cytoskeleton, which regulates cell polarity, adhesion, and migration, can influence cancer progression, including initial acquisition of malignant properties by normal cells, invasion of adjacent tissues, and metastasis to distant sites. Actin-dependent molecular motors, myosins, play key roles in regulating tumor progression and metastasis. In this review, we examine how non-muscle myosins regulate neoplastic transformation and cancer cell migration and invasion. Members of the myosin superfamily can act as either enhancers or suppressors of tumor progression. This review summarizes the current state of knowledge on how mutations or epigenetic changes in myosin genes and changes in myosin expression may affect tumor progression and patient outcomes and discusses the proposed mechanisms linking myosin inactivation or upregulation to malignant phenotype, cancer cell migration, and metastasis. © 2014 Wiley Periodicals, Inc.
    Cytoskeleton 08/2014; 71(8). DOI:10.1002/cm.21187 · 3.12 Impact Factor
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