NEW EMBO MEMBER'S REVIEW: The integrin-actin connection, an eternal love affair

Brakebusch, Cord

doi:10.1093/emboj/cdg245

Cited by 432 publications

(345 citation statements)

References 122 publications

(126 reference statements)

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“…Limited localization of PAT-3 ␤-integrin to the dense bodies in the myoepithelial sheath is a remarkable difference from its localization to both dense bodies and M-lines in the body wall muscle. Integrin plays critical roles in mediating extracellular signals to trigger several intracellular signaling events, including reorganization of the actin cytoskeleton (Brakebusch and Fassler, 2003;Wozniak et al, 2004;Lo, 2006). Thus, the difference in the integrin localization between striated and nonstriated muscles suggests that integrin has different functions in these muscles.…”

Section: Discussionmentioning

confidence: 99%

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Ono

2007

Developmental Dynamics

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Ovulation in the nematode Caenorhabditis elegans is regulated by complex signal transduction pathways and cell-cell interactions. Myoepithelial sheath cells of the proximal ovary are smooth muscle-like cells that provide contractile forces to push a mature oocyte into the spermatheca for fertilization. Although several genes that regulate sheath contraction have been characterized, basic components of the contractile apparatuses of the myoepithelial sheath have not been extensively studied. We identified major structural proteins of the contractile apparatuses of the myoepithelial sheath and characterized their nonstriated arrangement. Of interest, integrin and perlecan were found only at the dense bodies, whereas they localized to both dense bodies and M-lines in the striated body wall muscle. RNA interference of most of the myofibrillar components impaired ovulation in a soma-specific manner. Our results provide basic information that helps understanding the mechanism of sheath contraction during ovulation and establishing a new model to study morphogenesis of nonstriated muscle. Developmental Dynamics 236: 1093-1105, 2007.

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Section: Discussionmentioning

confidence: 99%

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Ono

2007

Developmental Dynamics

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“…Migration is a coordinated process that involves rapid changes in the dynamics of actin filaments, together with the formation and disassembly of cell adhesion sites (Brakebusch and Fassler, 2003). The interplay between the actin cytoskeleton and cell adhesion sites leads to the generation of membrane protrusions and traction forces (DeMali et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells

et al. 2007

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Prolactin (PRL) stimulates the cytoskeletal re-organization and motility of breast cancer cells. During PRL receptor signaling, Vav2 becomes phosphorylated and activated, an event regulated by the serine/threonine kinase Nek3. Given the regulatory role of Vav2, the function of Nek3 in PRL-mediated motility and invasion was examined. Overexpression of Nek3 in Chinese hamster ovary transfectants potentiated cytoskeletal re-organization in response to PRL. In contrast, downregulation of Nek3 expression by small-interfering RNA (siRNA) attenuated PRL-mediated cytoskeletal reorganization, activation of GTPase Rac1, cell migration and invasion of T47D cells. In addition, PRL stimulation induced an interaction between Nek3 and paxillin and significantly increased paxillin serine phosphorylation, whereas Nek3 siRNA-transfected cells showed a marked reduction in paxillin phosphorylation. Analysis of breast tissue microarrays also demonstrated a significant up-regulation of Nek3 expression in malignant versus normal specimens. These data suggest that Nek3 contributes to PRLmediated breast cancer motility through mechanisms involving Rac1 activation and paxillin phosphorylation.

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“…These signals promote protrusion of the cell membrane during cell spreading to allow formation of new actin-associated adhesion sites [1]. The integrin β subunit cytoplasmic domain (β tail) contributes to these processes by linking integrins to the actin cytoskeleton and to intracellular signaling cascades [2][3][4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Tac-β1 inhibits FAK activation and Src signaling

Berrier

Jones

LaFlamme

2008

Biochemical and Biophysical Research Communications

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The binding of integrins to extracellular matrix triggers signals that promote cell spreading. We previously demonstrated that expression of the integrin β1 cytoplasmic domain in the context of a chimeric transmembrane receptor with the Tac subunit of the interleukin-2 receptor (Tac-β1) inhibits cell spreading. To study the mechanism whereby Tac-β1-inhibits cell spreading, we examined the effect of Tac-β1 on early signaling events following integrin engagement namely FAK and Src signaling. We infected primary fibroblasts with adenoviruses expressing Tac or Tac-β1 and found that Tac-β1 prevented FAK activation by inhibiting the phosphorylation of FAK at Tyr-397. In contrast, Src activation was maintained, as phosphorylation of Src at Tyr-419 and Tyr-530 were not responsive to expression of Tac-β1. Importantly, adhesion-induced tyrosine phosphorylation of the Src substrates p130Cas and paxillin was inhibited, indicating that Src signaling was blocked by Tac-β1. These Src-dependent signaling events were found to require FAK signaling. Our results suggest that Tac-β1 inhibits cell spreading, at least in part, by preventing the phosphorylation of FAK at Tyr-397 and the assembly of signaling complexes necessary for phosphorylation of p130Cas and other downstream effectors.

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NEW EMBO MEMBER'S REVIEW: The integrin-actin connection, an eternal love affair

Cited by 432 publications

References 122 publications

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization and motility of breast cancer cells

Tac-β1 inhibits FAK activation and Src signaling

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