SH3 Domains

Mayer, Bruce J.; Saksela, Kalle

doi:10.1002/3527603611.ch2

Cited by 14 publications

(12 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The C-terminal 47-residue repeats of EspF U each contain an amphipathic helix that interacts with WASP/N-WASP (18,20), as well as a region that harbors up to 3 copies of the sequence PxxP, a motif associated with recognition by SH3 domaincontaining proteins (22). To identify possible SH3 domaincontaining host proteins that could link EspF U and Tir, we screened an essentially complete collection of human SH3 domains expressed on phage surface (23) for the ability to bind to GST-EspF U C, a GST fusion protein containing 6 Cterminal proline-rich repeats of EspF U [supporting information (SI) Fig.…”

Section: Resultsmentioning

confidence: 99%

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation

Vingadassalom

Kazlauskas

Skehan

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

112

132

View full text Add to dashboard Cite

Section: Resultsmentioning

confidence: 99%

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation

Vingadassalom

Kazlauskas

Skehan

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

112

132

View full text Add to dashboard Cite

“…It binds proline-rich sequences, which often contain the consensus sequence proline-x-x-proline (for reviews, see Refs. 10,11). SH3 domains are typically found in proteins involved in signal transduction, membrane trafficking, and cytoskeletal organization.…”

mentioning

confidence: 99%

Reciprocal Regulation of SH3 and SH2 Domain Binding via Tyrosine Phosphorylation of a Common Site in CD3ε

Kesti

Ruppelt

Wang

et al. 2007

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

Recruitment of cellular signaling proteins by the CD3 polypeptides of the TCR complex mediates T cell activation. We have screened a human Src homology 3 (SH3) domain phage display library for proteins that can bind to the proline-rich region of CD3ε. This screening identified Eps8L1 (epidermal growth factor receptor pathway substrate 8-like 1) together with the N-terminal SH3 domain of Nck1 and Nck2 as its preferred SH3 partners. Studies with recombinant proteins confirmed strong binding of CD3ε to Eps8L1 and Nck SH3 domains. CD3ε bound well also to Eps8 and Eps8L3, and modestly to Eps8L2, but not detectably to other SH3 domains tested. Interestingly, binding of Nck and Eps8L1 SH3 domains was mapped to a PxxDY motif that shared its tyrosine residue (Y166) with the ITAM of CD3ε. Phosphorylation of this residue abolished binding of Eps/Nck SH3 domains in peptide spot filter assays, as well as in cells cotransfected with a dominantly active Lck kinase. TCR ligation-induced binding and phosphorylation-dependent loss of binding were also demonstrated between Eps8L1 and endogenous CD3ε in Jurkat T cells. Thus, phosphorylation of Y166 serves as a molecular switch during T cell activation that determines the capacity of CD3ε to interact with either SH3 or SH2 domain-containing proteins.

show abstract

“…It has also been observed that small linear motifs tend to accumulate in protein regions predicted to be intrinsically disordered [30] and that proline-rich regions are usually devoid of secondary structure [31]. In most structures that we are aware of, the SH3 domain is in complex only with short target peptides, and not with full proteins.…”

Section: Introductionmentioning

confidence: 99%

Comparative Genomics and Disorder Prediction Identify Biologically Relevant SH3 Protein Interactions

Beltrão¹,

Serrano²

2005

PLoS Comput Biol

View full text Add to dashboard Cite

Protein interaction networks are an important part of the post-genomic effort to integrate a part-list view of the cell into system-level understanding. Using a set of 11 yeast genomes we show that combining comparative genomics and secondary structure information greatly increases consensus-based prediction of SH3 targets. Benchmarking of our method against positive and negative standards gave 83% accuracy with 26% coverage. The concept of an optimal divergence time for effective comparative genomics studies was analyzed, demonstrating that genomes of species that diverged very recently from Saccharomyces cerevisiae (S. mikatae, S. bayanus, and S. paradoxus), or a long time ago (Neurospora crassa and Schizosaccharomyces pombe), contain less information for accurate prediction of SH3 targets than species within the optimal divergence time proposed. We also show here that intrinsically disordered SH3 domain targets are more probable sites of interaction than equivalent sites within ordered regions. Our findings highlight several novel S. cerevisiae SH3 protein interactions, the value of selection of optimal divergence times in comparative genomics studies, and the importance of intrinsic disorder for protein interactions. Based on our results we propose novel roles for the S. cerevisiae proteins Abp1p in endocytosis and Hse1p in endosome protein sorting.

show abstract

SH3 Domains

Cited by 14 publications

References 49 publications

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation

Reciprocal Regulation of SH3 and SH2 Domain Binding via Tyrosine Phosphorylation of a Common Site in CD3ε

Comparative Genomics and Disorder Prediction Identify Biologically Relevant SH3 Protein Interactions

Contact Info

Product

Resources

About

SH3 Domains

Cited by 14 publications

References 49 publications

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspFUduring pedestal formation

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspFUduring pedestal formation

Reciprocal Regulation of SH3 and SH2 Domain Binding via Tyrosine Phosphorylation of a Common Site in CD3ε

Comparative Genomics and Disorder Prediction Identify Biologically Relevant SH3 Protein Interactions

Contact Info

Product

Resources

About

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation

Insulin receptor tyrosine kinase substrate links theE. coliO157:H7 actin assembly effectors Tir and EspF_Uduring pedestal formation