Does Vav bind to F‐actin through a CH domain?

Castresana, José; Saraste, Matti

doi:10.1016/0014-5793(95)01098-y

Cited by 140 publications

(99 citation statements)

References 17 publications

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“…Our results identifying Vav as a crucial actor in the SHP-1-mediated Fas signaling (Figures 3 and 4), together with both the well-known role of Vav in cytoskeletal rearrangement, and its ability to interact with actin, 29 (Figure 5d), explaining the sustained formation of Fas-actin association after prolonged stimulation (Figure 5c). …”

Section: Shp-1 Influences Fas-induced Cell Death By Modulatingsupporting

confidence: 54%

Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling

et al. 2007

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The actin cytoskeleton association is required for caspase 8-independent Fas/CD95 receptor internalization, a critical step for an optimal death-inducing signaling complex formation along the endocytic pathway, leading to efficient activation of the caspase cascade and, ultimately, cell death. However, the way in which this initiation phase of Fas receptor signaling is regulated is still unknown. We report herein that, in B cells, upon Fas engagement, the tyrosine phosphatase SHP-1-regulated Vav dephosphorylation, by downmodulating the Fas-ezrin-actin linkage is a fine-tune switch-off mechanism that the cell uses as a way to terminate the receptor internalization, controlling therefore the time and extent of the DISC formation and cell death.

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Section: Shp-1 Influences Fas-induced Cell Death By Modulatingsupporting

confidence: 54%

Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling

et al. 2007

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“…The domain distribution of this catalogue ( Figure 1B) illustrates the presence of various known and well-studied RNA binding domains like RRM (RNA recognition motif) [30], K-homology (KH) [31,32], DEAD/DEAH box [33], dsrm [34], WD40 [35] in addition to unclassified domains like the Pkinase domain of EIF2AK2 that auto phosphorylates upon binding of RNA to the dsRBD domain of EIF2AK2 [36,37]. Also notable is the Calponin homology (CH) domain found in both cytoskeletal and signalling proteins [38]. Further, superfamilies like the RNA binding domain, KH domain type-1, CCCH zinc finger were found to be enriched in RBPs when compared to the Non-RBPs (p<2.2e-16, Fisher's exact test) ( Figure 1C).…”

Section: Resultsmentioning

confidence: 99%

The human RBPome: From genes and proteins to human disease

Neelamraju

Hashemikhabir

Janga

2015

Journal of Proteomics

110

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“…A tandem pair of CH domains, each consisting of about 100 amino acids, has been suggested to confer actin binding on a variety of cytoskeletal and signaling events (31). Although a BLAST search against EB1 failed to find sequence similarity with other CH domains, some of the aromatic residues in the En core region are conserved throughout the CH domain family (Fig.…”

Section: Resultsmentioning

confidence: 99%

Crystal Structure of the Amino-terminal Microtubule-binding Domain of End-binding Protein 1 (EB1)

Hayashi

Ikura

2003

Journal of Biological Chemistry

168

145

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The end-binding protein 1 (EB1) family is a highly conserved group of proteins that localizes to the plusends of microtubules. EB1 has been shown to play an important role in regulating microtubule dynamics and chromosome segregation, but its regulation mechanism is poorly understood. We have determined the 1.45-Å resolution crystal structure of the amino-terminal domain of EB1, which is essential for microtubule binding, and show that it forms a calponin homology (CH) domain fold that is found in many proteins involved in the actin cytoskeleton. The functional CH domain for actin binding is a tandem pair, whereas EB1 is the first example of a single CH domain that can associate with the microtubule filament. Although our biochemical study shows that microtubule binding of EB1 is electrostatic in part, our mutational analysis suggests that the hydrophobic network, which is partially exposed in our crystal structure, is also important for the association. We propose that, like other actin-binding CH domains, EB1 employs the hydrophobic interaction to bind to microtubules.

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Does Vav bind to F‐actin through a CH domain?

Cited by 140 publications

References 17 publications

Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling

Regulating Vav1 phosphorylation by the SHP-1 tyrosine phosphatase is a fine-tuning mechanism for the negative regulation of DISC formation and Fas-mediated cell death signaling

The human RBPome: From genes and proteins to human disease

Crystal Structure of the Amino-terminal Microtubule-binding Domain of End-binding Protein 1 (EB1)

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