Arg Kinase-binding Protein 2 (ArgBP2) Interaction with α-Actinin and Actin Stress Fibers Inhibits Cell Migration

Anekal, Praju Vikas; Yong, Jeffery; Manser, Ed

doi:10.1074/jbc.m114.610725

Cited by 36 publications

(39 citation statements)

References 53 publications

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“…S1A). As the plasticity of ArgBP2 expression has been reported (Anekal et al, 2015), it remained possible that there was a small population of DKO MEFs expressing ArgBP2, even though ArgBP2 expression was not detected by immunoblotting. To overcome this possibility, a lentivirus expressing shRNA against ArgBP2 was transduced into DKO MEFs to stably knock down residual ArgBP2.…”

Section: Establishment Of Sorbs-re-expressing Cellsmentioning

confidence: 99%

“…These three SORBS proteins share binding partners, including vinculin (Kioka et al, 1999;Mandai et al, 1999;Cestra et al, 2005), the tyrosine kinase c-Abl (Wang et al, 1997;Lin et al, 2001;Mitsushima et al, 2006b), the E3 ubiquitin-protein ligase c-Cbl (Ribon et al, 1998b;Soubeyran et al, 2003;Mitsushima et al, 2006c) and the lipid raft protein flotillin (Kimura et al, 2001;Haglund et al, 2004). Among the vinexin family, only ArgBP2 is reported to interact with the actin crosslinking protein α-actinin (Rönty et al, 2005;Anekal et al, 2015). In addition to the function of vinexin-α as a mechanosensor, several studies have also demonstrated that SORBS proteins play roles in mechanotransduction: ArgBP2 increases phosphorylation of myosin regulatory light chain II (MRLC) (Martin et al, 2013), and the only orthologue in Drosophila, dCAP, regulates the assembly and function of tension-sensitive organs (Bharadwaj et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Vinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation

Ichikawa

Kita

Matsui

et al. 2017

Journal of Cell Science

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Vinexin, c-Cbl associated protein (CAP) and Arg-binding protein 2 (ArgBP2) constitute an adaptor protein family called the vinexin (SORBS) family that is targeted to focal adhesions (FAs). Although numerous studies have focused on each of the SORBS proteins and partially elucidated their involvement in mechanotransduction, a comparative analysis of their function has not been well addressed. Here, we established mouse embryonic fibroblasts that individually expressed SORBS proteins and analysed their functions in an identical cell context. Both vinexin-α and CAP co-localized with vinculin at FAs and promoted the appearance of vinculin-rich FAs, whereas ArgBP2 co-localized with α-actinin at the proximal end of FAs and punctate structures on actin stress fibers (SFs), and induced paxillin-rich FAs. Furthermore, both vinexin-α and CAP contributed to extracellular matrix stiffness-dependent vinculin behaviors, while ArgBP2 stabilized α-actinin on SFs and enhanced intracellular contractile forces. These results demonstrate the differential roles of SORBS proteins in mechanotransduction.

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Section: Establishment Of Sorbs-re-expressing Cellsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Vinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation

Ichikawa

Kita

Matsui

et al. 2017

Journal of Cell Science

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“…12,13 A recent report identified SORBS2 as being implicated in cancer progression. [14][15][16] However, the expression patterns, potential function and underlying mechanism of SORBS2 in HCC remain unknown.…”

Section: Introductionmentioning

confidence: 99%

The RNA‐binding protein SORBS2 suppresses hepatocellular carcinoma tumourigenesis and metastasis by stabilizing RORA mRNA

Han

Huang

Zhang

2019

Liver International

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Background Numerous studies have revealed that dysregulation of RNA‐binding protein (RBP) expression is causally linked with human cancer tumourigenesis. However, the detailed biological effect and underlying mechanisms of most RBPs remain unclear. Methods Expression of sorbin and SH3 domain‐containing 2 (SORBS2) in hepatocellular carcinoma (HCC) was detected by qRT‐PCR, immunohistochemistry assay and Western blot assay. Proliferation, migration, invasion and cell cycle progression of HCC cells were measured by 3‐(4,5‐Dimethylthiazol‐2‐yl)‐2,5‐diphenyltetrazolium bromide assay, colony‐forming assay, Transwell assay and flow cytometry assay respectively. A xenograft model and metastatic model were established to evaluate the proliferation and metastasis of HCC cells in vivo. Western blot assays were performed to assess the expression of epithelial‐mesenchymal transition markers. Luciferase reporter assay, RNA immunoprecipitation and pull‐down assay elucidated the effect of SORBS2 on one of its downstream genes. Results The expression of SORBS2 was significantly decreased in HCC and was associated with metastasis, advanced TNM clinical stage and poor clinical outcome of HCC patients. Furthermore, our results suggested that SORBS2 inhibited HCC cell proliferation, invasion, migration and EMT both in vivo and in vitro. Mechanistically, we revealed that retinoic acid receptor‐related orphan receptor (RORA) was a major target of SORBS2 and was critical to sustaining the antitumour effect of SORBS2 on HCC cells. SORBS2 reduced RORA mRNA degradation by directly binding to the 3′UTR of RORA mRNA. Conclusions In this study, we found for the first time that SORBS2 contributed to the suppression of HCC tumourigenesis and metastasis via post‐transcriptional regulation of RORA expression as an RBP.

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“…On the other hand, α-actinin1 (ACTN 1) is one of the major actin cross-linking proteins and anchors actin filaments to junctional structures and has an important role in some cellular biological processes such as cytokinesis, cell adhesion and cell migration (Murphy and Young, 2015). Recent evidence implicates that Sorbs2 can interact with α-actinin, subsequently binding to actin filaments (Rönty et al, 2005; Anekal et al, 2015). The current study is the first one describing interactions between the α-actinin1, Sorbs2 and JMY triad in Sertoli cells.…”

Section: Discussionmentioning

confidence: 99%

Functional importance of JMY expression by Sertoli cells in mediating mouse spermatogenesis

Fan

Yan

et al. 2018

Preprint

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3Sertoli cells are crucial for spermatogenesis in the seminiferous epithelium because 2 4 their actin cytoskeleton supports vesicle transport, cell junction, protein anchoring and 2 5 spermiation. Here, we show that junction-mediating and regulatory protein (JMY), an 2 6 actin regulating protein, also affects endocytic vesicle trafficking and Sertoli cell 2 7 junction remodeling since disruption of these functions induced male subfertility in 2 8Sertoli cell-specific Jmy knockout mice. Specifically, these mice have: a) impaired 2 9 BTB integrity and spermatid adhesion in the seminiferous tubules; b) high incidence 3 0 of sperm structural deformity; c) reduced sperm count and poor sperm motility. 3 1 Moreover, the cytoskeletal integrity in Sertoli cell-specific Jmy knockout mice was 3 2 compromised along with endocytic vesicular trafficking. These effects impaired 3 3 junctional protein recycling and reduced Sertoli cell junctions. In addition, JMY 3 4 interaction with α -actinin1 and Sorbs2 was related to JMY activity and in turn actin 3 5 cytoskeletal organization. In summary, JMY affects control of spermatogenesis 3 6 through regulating actin filament organization and endocytic vesicle trafficking in 3 7 Sertoli cells. 3 8 3 9

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Arg Kinase-binding Protein 2 (ArgBP2) Interaction with α-Actinin and Actin Stress Fibers Inhibits Cell Migration

Cited by 36 publications

References 53 publications

Vinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation

Vinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation

The RNA‐binding protein SORBS2 suppresses hepatocellular carcinoma tumourigenesis and metastasis by stabilizing RORA mRNA

Functional importance of JMY expression by Sertoli cells in mediating mouse spermatogenesis

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