Identification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1

Sato, Mariko; Maruoka, Masahiro; Yokota, Naohiko; Kuwano, Masayoshi; Matsui, Akira; Inada, Mika; Ogawa, Teiichiro; Ishida-Kitagawa, Norihiro; Takeya, Tatsuo

doi:10.1016/j.febslet.2011.02.012

Cited by 11 publications

(13 citation statements)

References 26 publications

(41 reference statements)

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“…Abi2 binds to c-Abl via dual proline-rich sequence/SH3 domain interaction and contacts between phosphorylated tyrosine of Abi2 and c-Abl SH2 (Dai and Pendergast 1995;Shi et al 2010). Phosphorylation of the SH3 domain of Abi-1 mediates Abl-Abi1 interaction and contributes to altered cell adhesion (Sato et al 2011).…”

Section: Regulationmentioning

confidence: 99%

SH3 domains: modules of protein–protein interactions

2012

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Src homology 3 (SH3) domains are involved in the regulation of important cellular pathways, such as cell proliferation, migration and cytoskeletal modifications. Recognition of polyproline and a number of noncanonical sequences by SH3 domains has been extensively studied by crystallography, nuclear magnetic resonance and other methods. High-affinity peptides that bind SH3 domains are used in drug development as candidates for anticancer treatment. This review summarizes the latest achievements in deciphering structural determinants of SH3 function.

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Section: Regulationmentioning

confidence: 99%

SH3 domains: modules of protein–protein interactions

2012

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“…How the phosphorylation of Abi by Abl and/or autophosphorylation of Abl play roles in these steps remains to be elucidated. Regarding this, several tyrosine phosphorylation sites have been identified in Abi1 [86–90]. Among them, Y213 [89] and Y398 [90] were reported to play a role in the regulation of Abl (Figure 4(a)).…”

Section: Regulation Of Abl Kinase By Abi and Crkmentioning

confidence: 99%

“…Regarding this, several tyrosine phosphorylation sites have been identified in Abi1 [86–90]. Among them, Y213 [89] and Y398 [90] were reported to play a role in the regulation of Abl (Figure 4(a)). Regarding this, preferred Abl target sites have been identified as I/V/L- Y -x 1-5 -P/F using an mRNA display method [91].…”

Section: Regulation Of Abl Kinase By Abi and Crkmentioning

confidence: 99%

“…Therefore, the significance of Y213 in the regulation of Abl awaits further clarification. Y398 in the SH3 domain of Abi1, on the other hand, was recently identified as another major site of phosphorylation by Abl [90]. Y398, located in the RT-loop of the SH3 domain, is highly conserved among other SH3 domain-containing proteins and presumed to play a role in the binding of target peptides [95].…”

Section: Regulation Of Abl Kinase By Abi and Crkmentioning

confidence: 99%

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Functional Mechanisms and Roles of Adaptor Proteins in Abl-Regulated Cytoskeletal Actin Dynamics

Sato

Maruoka

Takeya

2012

Journal of Signal Transduction

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Abl is a nonreceptor tyrosine kinase and plays an essential role in the modeling and remodeling of F-actin by transducing extracellular signals. Abl and its paralog, Arg, are unique among the tyrosine kinase family in that they contain an unusual extended C-terminal half consisting of multiple functional domains. This structural characteristic may underlie the role of Abl as a mediator of upstream signals to downstream signaling machineries involved in actin dynamics. Indeed, a group of SH3-containing accessory proteins, or adaptor proteins, have been identified that bind to a proline-rich domain of the C-terminal portion of Abl and modulate its kinase activity, substrate recognition, and intracellular localization. Moreover, the existence of signaling cascade and biological outcomes unique to each adaptor protein has been demonstrated. In this paper, we summarize functional roles and mechanisms of adaptor proteins in Abl-regulated actin dynamics, mainly focusing on a family of adaptor proteins, Abi. The mechanism of Abl's activation and downstream signaling mediated by Abi is described in comparison with those by another adaptor protein, Crk.

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“…binds Wave proteins, ␣4 integrin, the formin proteins Diaphanous1/2, and Nap1; or the C-terminal SH3 domain, which binds N-Wasp and c-Abl1 (5,9,18,(31)(32)(33). These constructs (wild-type abi1, abi1(⌬18 -145), or abi1 ⌬SH3) were introduced along with Abi1 MO into the D1.1.1 blastomere of embryos to test the ability of these mutants to rescue the eye defects caused by loss of Abi1.…”

Section: Knockdown Of Abi1 In X Laevis Affects Eye Development-be-mentioning

confidence: 99%

Abelson Interactor 1 (Abi1) and Its Interaction with Wiskott-Aldrich Syndrome Protein (Wasp) Are Critical for Proper Eye Formation in Xenopus Embryos

Singh

Winterbottom

et al. 2013

Journal of Biological Chemistry

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Abl interactor 1 (Abi1) is a scaffold protein that plays a central role in the regulation of actin cytoskeleton dynamics as a constituent of several key protein complexes, and homozygous loss of this protein leads to embryonic lethality in mice. Because this scaffold protein has been shown in cultured cells to be a critical component of pathways controlling cell migration and actin regulation at cell-cell contacts, we were interested to investigate the in vivo role of Abi1 in morphogenesis during the development of Xenopus embryos. Using morpholino-mediated translation inhibition, we demonstrate that knockdown of Abi1 in the whole embryo, or specifically in eye field progenitor cells, leads to disruption of eye morphogenesis. Moreover, signaling through the Src homology 3 domain of Abi1 is critical for proper movement of retinal progenitor cells into the eye field and their appropriate differentiation, and this process is dependent upon an interaction with the nucleation-promoting factor Wasp (Wiskott-Aldrich syndrome protein). Collectively, our data demonstrate that the Abi1 scaffold protein is an essential regulator of cell movement processes required for normal eye development in Xenopus embryos and specifically requires an Src homology 3 domain-dependent interaction with Wasp to regulate this complex morphogenetic process.

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Identification and functional analysis of a new phosphorylation site (Y398) in the SH3 domain of Abi-1

Cited by 11 publications

References 26 publications

SH3 domains: modules of protein–protein interactions

SH3 domains: modules of protein–protein interactions

Functional Mechanisms and Roles of Adaptor Proteins in Abl-Regulated Cytoskeletal Actin Dynamics

Abelson Interactor 1 (Abi1) and Its Interaction with Wiskott-Aldrich Syndrome Protein (Wasp) Are Critical for Proper Eye Formation in Xenopus Embryos

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