Regulating Rap small G-proteins in time and space

Gloerich, Martijn; Bos, Johannes L.

doi:10.1016/j.tcb.2011.07.001

Cited by 147 publications

(146 citation statements)

References 90 publications

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“…In addition, Rap1 activity can also trigger signaling via Radil or RAPL and may increase Arf6 inactivation by stimulating the GAP ARAP3. 44 Although strengthening of adhesive signaling usually triggers decreased motility, RhoA/B dKO neutrophils were highly motile without stimulation.…”

Section: Discussionmentioning

confidence: 99%

RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness

Jennings¹,

Strengert²,

Hayes³

et al. 2014

Blood

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Section: Discussionmentioning

confidence: 99%

RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness

Jennings¹,

Strengert²,

Hayes³

et al. 2014

Blood

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“…Rap1 is a small GTP-binding protein that cycles between an active, GTP-bound, and an inactive, GDP-bound state (Caron, 2003;Gloerich and Bos, 2011). Interestingly, Rap1 proteins are key regulators of phagocytosis and cell-cell adhesion.…”

Section: Mex3b Interacts With Rap1gapmentioning

confidence: 99%

The RNA-binding protein Mex3b regulates the spatial organization of the Rap1 pathway

et al. 2014

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The four related mammalian MEX-3 RNA-binding proteins are evolutionarily conserved molecules for which the in vivo functions have not yet been fully characterized. Here, we report that male mice deficient for the gene encoding Mex3b are subfertile. Seminiferous tubules of Mex3b-deficient mice are obstructed as a consequence of the disrupted phagocytic capacity of somatic Sertoli cells. In addition, both the formation and the integrity of the blood-testis barrier are compromised owing to mislocalization of N-cadherin and connexin 43 at the surface of Sertoli cells. We further establish that Mex3b acts to regulate the cortical level of activated Rap1, a small G protein controlling phagocytosis and cell-cell interaction, through the activation and transport of Rap1GAP. The active form of Rap1 (Rap1-GTP) is abnormally increased at the membrane cortex and chemically restoring Rap1-GTP to physiological levels rescues the phagocytic and adhesion abilities of Sertoli cells. Overall, these findings implicate Mex3b in the spatial organization of the Rap1 pathway that orchestrates Sertoli cell functions.

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“…Alternatively, syndecan-1 could be associating with guanine nucleotide exchange factors (GEFs) and/or GTPase-activating proteins (GAPs). Rap1 is controlled by cycling between a GTPbound (on) state and a GDP-bound (off) state, which is governed by GEFs and GAPs (Gloerich and Bos, 2011). Several Rap-1 GEFs and GAPs have PDZ domains that could associate with the PDZ binding domain on syndecan-1 to spatiotemporally control Rap1 (Nourry et al, 2003;García-Mata and Burridge, 2007).…”

Section: Syndecan-1 Regulates Fa Turnover 5191mentioning

confidence: 99%

Syndecan-1 controls cell migration by activating Rap1 to regulate focal adhesion disassembly

Altemeier

Schlesinger

Buell

et al. 2012

Journal of Cell Science

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SummaryAfter injury, residual epithelial cells coordinate contextual clues from cell-cell and cell-matrix interactions to polarize and migrate over the wound bed. Protrusion formation, cell body translocation and rear retraction is a repetitive process that allows the cell to move across the substratum. Fundamental to this process is the assembly and disassembly of focal adhesions that facilitate cell adhesion and protrusion formation. Here, we identified syndecan-1 as a regulator of focal adhesion disassembly in migrating lung epithelial cells. Syndecan-1 altered the dynamic exchange of adhesion complex proteins, which in turn regulates migration speed. Moreover, we provide evidence that syndecan-1 controls this entire process through Rap1. Thus, syndecan-1 restrains migration in lung epithelium by activating Rap1 to slow focal adhesion disassembly.

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Regulating Rap small G-proteins in time and space

Cited by 147 publications

References 90 publications

RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness

RhoA determines disease progression by controlling neutrophil motility and restricting hyperresponsiveness

The RNA-binding protein Mex3b regulates the spatial organization of the Rap1 pathway

Syndecan-1 controls cell migration by activating Rap1 to regulate focal adhesion disassembly

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