Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network

Almeida, Cláudia G.; Yamada, Ayako; Tenza, Danièle; Louvard, Daniel; Raposo, Graça; Coudrier, Evelyne

doi:10.1038/ncb2262

Cited by 112 publications

(164 citation statements)

References 49 publications

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“…In support of this hypothesis, motor activity of MYO5B is essential for the formation of Rab10 vesicles and axon development. In line with this model, myosin Ib has been shown to be a molecular force sensor 43,44 , and promotes the formation of tubular-carrier precursors 45 . Another example is myosin II, which has been shown to control fission of Rab6 vesicles at the Golgi complex 46 .…”

Section: Discussionmentioning

confidence: 84%

Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development

Liu

Chen

et al. 2013

Nat Commun

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Polarized membrane addition is crucial for axon development and elongation during neuronal morphogenesis. This process is believed to be regulated by directed membrane trafficking of Rab10-containing post-Golgi carriers. However, the mechanisms underlying the biogenesis of these carriers remain unclear. Here, we report that Rab10 interaction with myosin Vb (MYO5B) determines the formation of Rab10 carriers and is important for axon development. Rab10 interacts with the exon D-encoded domain of MYO5B. Downregulating the expression of MYO5B ( þ D) or blocking its interaction with Rab10 impairs the fission of Rab10 vesicles from trans-Golgi membranes, causes a decrease in the number of Rab10 transport carriers and inhibits axon development in cultured hippocampal neurons. Furthermore, the MYO5B-Rab10 system is required for axon development of vertebrate neocortical neurons or zebrafish retinal ganglion cells in vivo. Thus, specific interaction between Rab10 and MYO5B controls the formation of Rab10 vesicles, which is required for axon development.

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Section: Discussionmentioning

confidence: 84%

Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development

Liu

Chen

et al. 2013

Nat Commun

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“…The functional roles of Myo1b in cancer biology have not previously been known, although its association with cell migration of zebrafish embryo cells (11) and intracellular transport regulated by the formation of post-Golgi carriers were reported (12,13). Myo1b was reported to localize at plasma membrane structures, including filopodia, ruffles, and lamellipodia (38,39,44).…”

Section: Discussionmentioning

confidence: 99%

“…Myosin 1b (Myo1b, also named myosin 1 alpha or Myr1), a member of the myosin family, was found to be upregulated in HNSCC through a web-based bioinformatics meta-analysis. Myo1b, a class I myosin, is a widely expressed, single-headed, actin-associated molecular motor, associated with cell migration of zebrafish embryo cells (11) and intracellular transport regulated by the formation of post-Golgi carriers (12,13). However, its role in cancer biology has never been reported.…”

Section: Introductionmentioning

confidence: 99%

Aberrant Myosin 1b Expression Promotes Cell Migration and Lymph Node Metastasis of HNSCC

Ohmura

Tsujikawa

Yaguchi

et al. 2015

Molecular Cancer Research

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Lymph node metastasis is the major clinicopathologic feature associated with poor prognosis in patients with head and neck squamous cell carcinoma (HNSCC). Here, web-based bioinformatics meta-analysis was performed to elucidate the molecular mechanism of lymph node metastasis of human HNSCC. Preferential upregulation of Myosin 1b (MYO1B) transcript in HNSCC datasets was identified. Myo1b mRNA was highly expressed in human HNSCC cells and patient tissue specimens compared with their normal counterparts as shown by quantitative PCR (qPCR) analyses. Immunohistochemistry (IHC)-detected Myo1b expression was significantly correlated with lymph node metastases in patients with oral cancer of the tongue. HNSCC with high expression of Myo1b and chemokine receptor 4 (CCR4), another metastasis-associated molecule, was strongly associated with lymph node metastasis. RNA interference (RNAi) of Myo1b in HNSCC cells, SAS and HSC4, significantly inhibited migratory and invasive abilities through decreased large protrusion formation of cell membranes. Finally, Myo1b knockdown in SAS cells significantly inhibited in vivo cervical lymph node metastases in a cervical lymph node metastatic mouse model system. Implications: Myo1b is functionally involved in lymph node metastasis of human HNSCC through enhanced cancer cell motility and is an attractive target for new diagnostic and therapeutic strategies for patients with HNSCC.

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“…Eight class I myosins are expressed in humans and mice (Berg et al 2001). Myosin IA is thought to maintain brush border structure and membrane tension and to power the release of vesicles from the tips of microvilli (Tyska et al 2005;McConnell et al 2009;Nambiar et al 2009), while Myosin IB regulates the actin-dependent post-Golgi trafficking of cargo (Almeida et al 2011). Myosin IC is involved in vesicle transport both in the fertilized egg of Xenopus and in mammalian cells (Bose et al 2002;Sokac et al 2006;Fan et al 2012) and regulates ion channels in the hair cells of the inner ear (Gillespie and Cyr 2004).…”

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confidence: 99%

Class I Myosins Have Overlapping and Specialized Functions in Left-Right Asymmetric Development inDrosophila

et al. 2015

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The class I myosin genes are conserved in diverse organisms, and their gene products are involved in actin dynamics, endocytosis, and signal transduction. Drosophila melanogaster has three class I myosin genes, Myosin 31DF (Myo31DF), Myosin 61F (Myo61F), and Myosin 95E (Myo95E). Myo31DF, Myo61F, and Myo95E belong to the Myosin ID, Myosin IC, and Myosin IB families, respectively. Previous loss-of-function analyses of Myo31DF and Myo61F revealed important roles in left-right (LR) asymmetric development and enterocyte maintenance, respectively. However, it was difficult to elucidate their roles in vivo, because of potential redundant activities. Here we generated class I myosin double and triple mutants to address this issue. We found that the triple mutant was viable and fertile, indicating that all three class I myosins were dispensable for survival. A loss-of-function analysis revealed further that Myo31DF and Myo61F, but not Myo95E, had redundant functions in promoting the dextral LR asymmetric development of the male genitalia. Myo61F overexpression is known to antagonize the dextral activity of Myo31DF in various Drosophila organs. Thus, the LR-reversing activity of overexpressed Myo61F may not reflect its physiological function. The endogenous activity of Myo61F in promoting dextral LR asymmetric development was observed in the male genitalia, but not the embryonic gut, another LR asymmetric organ. Thus, Myo61F and Myo31DF, but not Myo95E, play tissue-specific, redundant roles in LR asymmetric development. Our studies also revealed differential colocalization of the class I myosins with filamentous (F)-actin in the brush border of intestinal enterocytes.KEYWORDS myosin I; Myosin 31DF; Myosin 61F; Myosin 95E; left-right asymmetry T HE class I myosin genes encode myosin heavy chains, which are conserved in phylogenetically diverse organisms (Sellers 2000;Krendel and Mooseker 2005). The class I myosins are nonfilamentous, actin-based motor proteins and were the first discovered unconventional myosin proteins. These myosins are involved in a variety of cellular processes, such as cell migration, cell adhesion, and cell growth, through their regulation of actin dynamics, endocytosis, and signal transduction (Osherov and May 2000;Krendel and Mooseker 2005;Kim and Flavell 2008;McConnell and Tyska 2010).The structure of the myosin I heavy chains is evolutionarily conserved and composed of head (or motor), neck, and tail domains ( Figure 1A) (Coluccio 1997;Barylko et al. 2000). The head domain binds to filamentous (F)-actin and adenosine triphosphate (ATP), a common feature of myosin proteins ( Figure 1A) (Mermall et al. 1998); the neck domain possesses one or more IQ motifs, which directly interact with calmodulin or calmodulin-related myosin light chains (Coluccio 1997;Barylko et al. 2000), and the tail domains are divided into short and long types. Short tails contain a single tail homology 1 (TH1) domain, which is rich in basic residues and thought to interact with plasma membranes (Coluccio 1997;Barylko...

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Myosin 1b promotes the formation of post-Golgi carriers by regulating actin assembly and membrane remodelling at the trans-Golgi network

Cited by 112 publications

References 49 publications

Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development

Myosin Vb controls biogenesis of post-Golgi Rab10 carriers during axon development

Aberrant Myosin 1b Expression Promotes Cell Migration and Lymph Node Metastasis of HNSCC

Class I Myosins Have Overlapping and Specialized Functions in Left-Right Asymmetric Development inDrosophila

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