ArticlePloS one2012
SH3 domain tyrosine phosphorylation--sites, role and evolution.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
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- A signaling inspired synthetic toolkit for efficient production of tyrosine phosphorylated proteins.bioRxiv : the preprint server for biology · 2025Article
- Mechanisms by which SNX-BAR subfamily controls the fate of SNXs' cargo.Frontiers in physiology · 2025Review
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- Gene-deficient mouse model established by CRISPR/Cas9 system reveals 15 reproductive organ-enriched genes dispensable for male fertility.Frontiers in cell and developmental biology · 2024Article
- Phosphorylation of tyrosine 90 in SH3 domain is a new regulatory switch controlling Src kinase.eLife · 2023Article
- Molecular and Functional Characterization of a Short-Type Peptidoglycan Recognition Protein, Ct-PGRP-S1 in the Giant Triton SnailInternational journal of molecular sciences · 2022Article
- Impact of a conserved N-terminal proline-rich region of the α-subunit of CAAX-prenyltransferases on their enzyme properties.Cell communication and signaling : CCS · 2022Article
- The conserved Pelado/ZSWIM8 protein regulates actin dynamics by promoting linear actin filament polymerization.Life science alliance · 2022Article
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- Itk Promotes the Integration of TCR and CD28 Costimulation through Its Direct Substrates SLP-76 and Gads.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Review
- Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions.The Journal of biological chemistry · 2019Article
- Direct Phosphorylation of SRC Homology 3 Domains by Tyrosine Kinase Receptors Disassembles Ligand-Induced Signaling Networks.Molecular cell · 2018Article
- NEDD9 stimulated MMP9 secretion is required for invadopodia formation in oral squamous cell carcinoma.Oncotarget · 2018Article
- Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.Scientific reports · 2017Article
- Isoelectric point-based fractionation by HiRIEF coupled to LC-MS allows for in-depth quantitative analysis of the phosphoproteome.Scientific reports · 2017Article
- The role of focal adhesion anchoring domains of CAS in mechanotransduction.Scientific reports · 2017Article
- Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.PloS one · 2015Article
- CAS directly interacts with vinculin to control mechanosensing and focal adhesion dynamics.Cellular and molecular life sciences : CMLS · 2014Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSH3 domains are eukaryotic protein domains that participate in a plethora of cellular processes including signal transduction, proliferation, and cellular movement. Several studies indicate that tyrosine phosphorylation could play a significant role in the regulation of SH3 domains.
resultsTo explore the incidence of the tyrosine phosphorylation within SH3 domains we queried the PhosphoSite Plus database of phosphorylation sites. Over 100 tyrosine phosphorylations occurring on 20 different SH3 domain positions were identified. The tyrosine corresponding to c-Src Tyr-90 was by far the most frequently identified SH3 domain phosphorylation site. A comparison of sequences around this tyrosine led to delineation of a preferred sequence motif ALYD(Y/F). This motif is present in about 15% of human SH3 domains and is structurally well conserved. We further observed that tyrosine phosphorylation is more abundant than serine or threonine phosphorylation within SH3 domains and other adaptor domains, such as SH2 or WW domains. Tyrosine phosphorylation could represent an important regulatory mechanism of adaptor domains.
conclusionsWhile tyrosine phosphorylation typically promotes signaling protein interactions via SH2 or PTB domains, its role in SH3 domains is the opposite - it blocks or prevents interactions. The regulatory function of tyrosine phosphorylation is most likely achieved by the phosphate moiety and its charge interfering with binding of polyproline helices of SH3 domain interacting partners.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.