p130Cas-dependent actin remodelling regulates myogenic differentiation

Kawauchi, Keiko; Tan, Wee Wee; Araki, Keigo; Bakar, Farhana B. Abu; Kim, Minsoo; Fujita, Hideaki; Harai, Hiroaki; Sawada, Yasuhiro

doi:10.1042/bj20112169

Cited by 26 publications

(33 citation statements)

References 48 publications

(77 reference statements)

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“…81 These findings indicate the role of p130Cas phosphorylation in regulating actin assembly/disassembly. On the other hand, we have also observed that p130Cas phosphorylation is markedly decreased when actin filaments are disrupted by treatment with cytochalasin D or latrunculin A (our unpublished observation), suggesting that the actin cytoskeleton plays a significant role in controlling p130Cas phosphorylation.…”

Section: Mutual Regulation Of the Actin Cytoskeleton And P130cas Phosmentioning

confidence: 82%

“…Furthermore, to move our body parts efficiently, our locomotive organs, that is, musculoskeletal systems, are required to respond to changes in motion and forces. Humans and animals therefore possess the molecular machinery for mechanosensing and mechanotransduction, and these include Src and p130Cas, both of which are involved in the normal differentiation of muscle 81,99 as well as bone cells 100,101 (Fig. 3A).…”

Section: Mechanical Regulation Of Src and P130cas Is Distinguished Bementioning

confidence: 99%

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Src, p130Cas, and Mechanotransduction in Cancer Cells

2012

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Anchorage-independent growth is the most significant hallmark of cell transformation, which has an intimate relevance to cancer. Anchorage or adhesion physically links cells to the extracellular matrix and allows the transmission of external mechanical cues to intracellular signaling machineries. Transformation involves acquiring the ability to proliferate without requiring mechanically initiated signal transduction, known as mechanotransduction. A number of signaling and cytoskeletal molecules are located at focal adhesions. Src and its related proteins, including p130Cas, localize to adhesion sites, where their functions can be mechanically regulated. In addition, the aberrant activation and expression of Src and p130Cas are linked to transformation and malignancy both in vitro and in vivo. These findings shed light on the importance of mechanotransduction in tumorigenesis and the regulation of cancer progression and also provide insights into the mechanical aspects of cancer signaling.

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Section: Mutual Regulation Of the Actin Cytoskeleton And P130cas Phosmentioning

confidence: 82%

Section: Mechanical Regulation Of Src and P130cas Is Distinguished Bementioning

confidence: 99%

Src, p130Cas, and Mechanotransduction in Cancer Cells

2012

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“…Filamins are also actin-binding proteins that function as F-actin crosslinkers (49). MICAL is also a binding protein of the P130 Cas family members Cas and CasL that have been implicated in the regulation of actin dynamics (26,33,78). MICAL also interacts with vimentin, which can lead to cytoskeletal alterations when oxidized by H 2 O 2 (64, 78).…”

Section: Giridharan and Caplanmentioning

confidence: 99%

MICAL-Family Proteins: Complex Regulators of the Actin Cytoskeleton

Giridharan

Caplan²

2014

Antioxidants & Redox Signaling

101

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Significance: The molecules interacting with CasL (MICAL) family members participate in a multitude of activities, including axonal growth cone repulsion, membrane trafficking, apoptosis, and bristle development in flies. An interesting feature of MICAL proteins is the presence of an N-terminal flavo-mono-oxygenase domain. This mono-oxygenase domain generates redox potential with which MICALs can either oxidize proteins or produce reactive oxygen species (ROS). Actin is one such protein that is affected by MICAL function, leading to dramatic cytoskeletal rearrangements. This review describes the MICAL-family members, and discusses their mechanisms of actin-binding and regulation of actin cytoskeleton organization. Recent Advances: Recent studies show that MICALs directly induce oxidation of actin molecules, leading to actin depolymerization. ROS production by MICALs also causes oxidation of collapsin response mediator protein-2, a microtubule assembly promoter, which subsequently undergoes phosphorylation. Critical Issues: MICAL proteins oxidize proteins through two mechanisms: either directly by oxidizing methionine residues or indirectly via the production of ROS. It remains unclear whether MICAL proteins employ both mechanisms or whether the activity of MICALfamily proteins might vary with different substrates. Future Directions: The identification of additional substrates oxidized by MICAL will shed new light on MICAL protein function. Additional directions include expanding studies toward the MICAL-like homologs that lack flavin adenine dinucleotide domains and oxidation activity.

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“…Cas and MAPK (Kawauchi et al, 2012). a7 integrin mutations result in congenital myopathies in humans and induce muscular dystrophy in mice (Hayashi et al, 1998;Mayer et al, 1997).…”

Section: Discussionmentioning

confidence: 99%

Bit-1 is an essential regulator of myogenic differentiation

Griffiths

Doe

Jijiwa

et al. 2015

Journal of Cell Science

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Muscle differentiation requires a complex signaling cascade that leads to the production of multinucleated myofibers. Genes regulating the intrinsic mitochondrial apoptotic pathway also function in controlling cell differentiation. How such signaling pathways are regulated during differentiation is not fully understood. Bit-1 (also known as PTRH2) mutations in humans cause infantile-onset multisystem disease with muscle weakness. We demonstrate here that Bit-1 controls skeletal myogenesis through a caspase-mediated signaling pathway. Bit-1-null mice exhibit a myopathy with hypotrophic myofibers. Bit-1-null myoblasts prematurely express muscle-specific proteins. Similarly, knockdown of Bit-1 expression in C2C12 myoblasts promotes early differentiation, whereas overexpression delays differentiation. In wildtype mice, Bit-1 levels increase during differentiation. Bit-1-null myoblasts exhibited increased levels of caspase 9 and caspase 3 without increased apoptosis. Bit-1 re-expression partially rescued differentiation. In Bit-1-null muscle, Bcl-2 levels are reduced, suggesting that Bcl-2-mediated inhibition of caspase 9 and caspase 3 is decreased. Bcl-2 re-expression rescued Bit-1-mediated early differentiation in Bit-1-null myoblasts and C2C12 cells with knockdown of Bit-1 expression. These results support an unanticipated yet essential role for Bit-1 in controlling myogenesis through regulation of Bcl-2.

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p130Cas-dependent actin remodelling regulates myogenic differentiation

Cited by 26 publications

References 48 publications

Src, p130Cas, and Mechanotransduction in Cancer Cells

Src, p130Cas, and Mechanotransduction in Cancer Cells

MICAL-Family Proteins: Complex Regulators of the Actin Cytoskeleton

Bit-1 is an essential regulator of myogenic differentiation

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