ArticleMolecular and cellular biology1999
Physiological requirement for both SH2 domains for phospholipase C-gamma1 function and interaction with platelet-derived growth factor receptors.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 67 citations in OpenAlex.
- Dynamics of allosteric regulation of the phospholipase C-γ isozymes upon recruitment to membranes.eLife · 2022Article
- Emerging roles of PLCγ1 in endothelial biology.Science signaling · 2021Review
- Recruitment of phospholipase Cγ1 to the non-structural membrane protein pK15 of Kaposi Sarcoma-associated herpesvirus promotes its Src-dependent phosphorylation.PLoS pathogens · 2021Article
- Combinatorial diversity of Syk recruitment driven by its multivalent engagement with FcεRIγ.Molecular biology of the cell · 2019Article
- Design and evaluation of engineered protein biosensors for live-cell imaging of EGFR phosphorylation.Science signaling · 2019Article
- Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Cold Spring Harbor perspectives in biology · 2013Review
- Article
- Semaphorin 4D signaling requires the recruitment of phospholipase C gamma into the plexin-B1 receptor complex.Molecular and cellular biology · 2009Article
- Out of the box binding determines specificity of SH2 domain interaction.Structure (London, England : 1993) · 2009Article
- Article
- PLC-gamma1 regulates fibronectin assembly and cell aggregation.Experimental cell research · 2009Article
- A genetic screen for vascular mutants in zebrafish reveals dynamic roles for Vegf/Plcg1 signaling during artery development.Developmental biology · 2009Article
- Role of phospholipase Cgamma1 in cell spreading requires association with a beta-Pix/GIT1-containing complex, leading to activation of Cdc42 and Rac1.Molecular and cellular biology · 2007Article
- The ErbB4 receptor in fetal rat lung fibroblasts and epithelial type II cells.Biochimica et biophysica acta · 2007Article
- Intramolecular regulation of phospholipase C-gamma1 by its C-terminal Src homology 2 domain.Molecular and cellular biology · 2007Article
- Structural basis for recognition of the T cell adaptor protein SLP-76 by the SH3 domain of phospholipase Cgamma1.Journal of molecular biology · 2005Article
- Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-gamma1.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- PIKE GTPase signaling and function.International journal of biological sciences · 2005Review
- Role of the pleckstrin homology domain of PLCgamma1 in its interaction with the insulin receptor.The Journal of cell biology · 2003Article
- Recruitment and activation of phospholipase Cgamma1 by vascular endothelial growth factor receptor-2 are required for tubulogenesis and differentiation of endothelial cells.The Journal of biological chemistry · 2003Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Two approaches have been utilized to investigate the role of individual SH2 domains in growth factor activation of phospholipase C-gamma1 (PLC-gamma1). Surface plasmon resonance analysis indicates that the individual N-SH2 and C-SH2 domains are able to specifically recognize a phosphotyrosine-containing peptide corresponding to Tyr 1021 of the platelet-derived growth factor (PDGF) beta receptor. To assess SH2 function in the context of the full-length PLC-gamma1 molecule as well as within the intact cell, PLC-gamma1 SH2 domain mutants, disabled by site-directed mutagenesis of the N-SH2 and/or C-SH2 domain(s), were expressed in Plcg1(-/-) fibroblasts. Under equilibrium incubation conditions (4 degrees C, 40 min), the N-SH2 domain, but not the C-SH2 domain, was sufficient to mediate significant PLC-gamma1 association with the activated PDGF receptor and PLC-gamma1 tyrosine phosphorylation. When both SH2 domains in PLC-gamma1 were disabled, the double mutant did not associate with activated PDGF receptors and was not tyrosine phosphorylated. However, no single SH2 mutant was able to mediate growth factor activation of Ca2+ mobilization or inositol 1,4,5-trisphosphate (IP3) formation. Subsequent kinetic experiments demonstrated that each single SH2 domain mutant was significantly impaired in its capacity to mediate rapid association with activated PDGF receptors and become tyrosine phosphorylated. Hence, when assayed under physiological conditions necessary to achieve a rapid biological response (Ca2+ mobilization and IP3 formation), both SH2 domains of PLC-gamma1 are essential to growth factor responsiveness.
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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.