Myosin VI is associated with secretory granules and is present in the nucleus in adrenal medulla chromaffin cells.

Majewski, Łukasz; Sobczak, Magdalena; Rędowicz, Maria Jolanta

doi:10.18388/abp.2010_2381

Cited by 12 publications

(19 citation statements)

References 34 publications

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“…This is in line with our earlier observation that MVI localizes to the endoplasmic reticulum of neurosecretory PC12 cells (Majewski et al 2010). Moreover, we detected MVI in the SR fractions isolated from both rat fast twitch muscle and cardiac ventricular muscle.…”

Section: Discussionsupporting

confidence: 93%

“…The presence of MVI within the nucleus has been already reported for many cancer cell lines, including neurosecretory pheochromocytoma PC12 cells, prostate cancer and HeLa cells (Vreugde et al 2006; Jung et al 2006; Majewski et al 2010). Interestingly, non-muscle actin and at least four other unconventional myosins have been found within the nucleus, where they play important roles in transcription and nuclear transport (de Lanerolle and Serebryannyy 2011).…”

Section: Discussionmentioning

confidence: 74%

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Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei

Karolczak

Sobczak

Majewski

et al. 2012

Histochem Cell Biol

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Myosin VI (MVI) is a unique unconventional motor moving backwards on actin filaments. In non-muscle cells, it is involved in cell migration, endocytosis and intracellular trafficking, actin cytoskeleton dynamics, and possibly in gene transcription. An important role for MVI in striated muscle functioning was suggested in a report showing that a point mutation (H236R) within the MVI gene was associated with cardiomyopathy (Mohiddin et al., J Med Genet 41:309–314, 2004). Here, we have addressed MVI function in striated muscle by examining its expression and distribution in rat hindlimb skeletal muscle. We found that MVI was present predominantly at the muscle fiber periphery, and it was also localized within muscle nuclei. Analysis of both the hindlimb and cardiac muscle longitudinal sections revealed ~3 μm striation pattern, corresponding to the sarcoplasmic reticulum. Moreover, MVI was detected in the sarcoplasmic reticulum fractions isolated from skeletal and cardiac muscle. The protein also localized to the postsynaptic region of the neuromuscular junction. In denervated muscle, the defined MVI distribution pattern was abolished and accompanied by significant increase in its amount in the muscle fibers. In addition, we have identified several novel potential MVI-binding partners, which seem to aid our observations that in striated muscle MVI could be involved in postsynaptic trafficking as well as in maintenance of and/or transport within the sarcoplasmic reticulum and non-sarcomeric cytoskeleton.Electronic supplementary materialThe online version of this article (doi:10.1007/s00418-012-1070-9) contains supplementary material, which is available to authorized users.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionmentioning

confidence: 74%

Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei

Karolczak

Sobczak

Majewski

et al. 2012

Histochem Cell Biol

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“…One of the best candidates to facilitate transport of vesicles derived from the Golgi and from the plasma membrane is MVI, which moves toward the minus end of actin filaments and is involved in both clathrin-mediated endocytosis and secretion (see review by Buss and Kendrick-Jones 2008 ). Interestingly, MVI-SI and MVI-NoI splice variants, the isoforms we detected in mouse testis, have previously been shown to play a role in transport of clathrin-coated as well as uncoated vesicles in different mammalian cell lines (Aschenbrenner et al 2003 ; Dance et al 2004 ; Naccache et al 2006 ; Au et al 2007 ; Chibalina et al 2007 ; Puri 2009 ; Majewski et al 2010 ; Bond et al 2012 ; Tumbarello et al 2012 ; Tomatis et al 2013 ). Given that plus ends of actin filaments typically are positioned towards cell membranes (Cramer 1999 ), MVI acting as a minus-end-directed motor would move vesicles away from the Golgi surface to the center of the cell.…”

Section: Discussionmentioning

confidence: 78%

“…Additionally, a central role of MVI in exocytosis, including the Golgi ribbon formation and sorting of proteins into different cargo vesicles has been suggested. Specifically, MVI concentration in the TGN is thought to facilitate post-Golgi secretion, including vesicle formation and budding, and then fusion of secretory vesicles with the plasma membrane during the final stage of exocytosis (Buss et al 1998 ; Warner et al 2003 ; Au et al 2007 ; Majewski et al 2010 ; Bond et al 2011 ; Tomatis et al 2013 ). Thus, association of MVI with the Golgi apparatus, coated, and uncoated vesicles argue that MVI may be involved in the anterograde and/or the retrograde vesicular transport pathways during acrosome biogenesis in mouse.…”

Section: Discussionmentioning

confidence: 99%

Expression and localization of myosin VI in developing mouse spermatids

Zakrzewski

Lenartowski

Rędowicz

et al. 2017

Histochem Cell Biol

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Myosin VI (MVI) is a versatile actin-based motor protein that has been implicated in a variety of different cellular processes, including endo- and exocytic vesicle trafficking, Golgi morphology, and actin structure stabilization. A role for MVI in crucial actin-based processes involved in sperm maturation was demonstrated in Drosophila. Because of the prominence and importance of actin structures in mammalian spermiogenesis, we investigated whether MVI was associated with actin-mediated maturation events in mammals. Both immunofluorescence and ultrastructural analyses using immunogold labeling showed that MVI was strongly linked with key structures involved in sperm development and maturation. During the early stage of spermiogenesis, MVI is associated with the Golgi and with coated and uncoated vesicles, which fuse to form the acrosome. Later, as the acrosome spreads to form a cap covering the sperm nucleus, MVI is localized to the acroplaxome, an actin-rich structure that anchors the acrosome to the nucleus. Finally, during the elongation/maturation phase, MVI is associated with the actin-rich structures involved in nuclear shaping: the acroplaxome, manchette, and Sertoli cell actin hoops. Since this is the first report of MVI expression and localization during mouse spermiogenesis and MVI partners in developing sperm have not yet been identified, we discuss some probable roles for MVI in this process. During early stages, MVI is hypothesized to play a role in Golgi morphology and function as well as in actin dynamics regulation important for attachment of developing acrosome to the nuclear envelope. Next, the protein might also play anchoring roles to help generate forces needed for spermatid head elongation. Moreover, association of MVI with actin that accumulates in the Sertoli cell ectoplasmic specialization and other actin structures in surrounding cells suggests additional MVI functions in spermatid movement across the seminiferous epithelium and in sperm release.

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“…Together these lines of evidence point toward the possibility that myosin VI could regulate neuroexocytosis by anchoring/recruiting SVs to the actin network before they undergo fusion with the plasma membrane. Although little is known about the precise molecular mechanism(s) underpinning this role, the function of myosin VI in regulated in exocytosis in PC12 cells has been questioned (156). However, Drosophila mutants lacking myosin VI display altered neuromuscular junction morphology and synaptic vesicle localization resulting in impaired synaptic plasticity (157).…”

Section: Myosinsmentioning

confidence: 99%

The Cortical Acto-Myosin Network: From Diffusion Barrier to Functional Gateway in the Transport of Neurosecretory Vesicles to the Plasma Membrane

et al. 2013

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Dysregulation of regulated exocytosis is linked to an array of pathological conditions, including neurodegenerative disorders, asthma, and diabetes. Understanding the molecular mechanisms underpinning neuroexocytosis including the processes that allow neurosecretory vesicles to access and fuse with the plasma membrane and to recycle post-fusion, is therefore critical to the design of future therapeutic drugs that will efficiently tackle these diseases. Despite considerable efforts to determine the principles of vesicular fusion, the mechanisms controlling the approach of vesicles to the plasma membrane in order to undergo tethering, docking, priming, and fusion remain poorly understood. All these steps involve the cortical actin network, a dense mesh of actin filaments localized beneath the plasma membrane. Recent work overturned the long-held belief that the cortical actin network only plays a passive constraining role in neuroexocytosis functioning as a physical barrier that partly breaks down upon entry of Ca2+ to allow secretory vesicles to reach the plasma membrane. A multitude of new roles for the cortical actin network in regulated exocytosis have now emerged and point to highly dynamic novel functions of key myosin molecular motors. Myosins are not only believed to help bring about dynamic changes in the actin cytoskeleton, tethering and guiding vesicles to their fusion sites, but they also regulate the size and duration of the fusion pore, thereby directly contributing to the release of neurotransmitters and hormones. Here we discuss the functions of the cortical actin network, myosins, and their effectors in controlling the processes that lead to tethering, directed transport, docking, and fusion of exocytotic vesicles in regulated exocytosis.

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Myosin VI is associated with secretory granules and is present in the nucleus in adrenal medulla chromaffin cells.

Cited by 12 publications

References 34 publications

Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei

Myosin VI in skeletal muscle: its localization in the sarcoplasmic reticulum, neuromuscular junction and muscle nuclei

Expression and localization of myosin VI in developing mouse spermatids

The Cortical Acto-Myosin Network: From Diffusion Barrier to Functional Gateway in the Transport of Neurosecretory Vesicles to the Plasma Membrane

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