PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254

Kim, Ha Kun; Kim, Jae Won; Zilberstein, Asher; Margolis, Benjamin; Kim, Jin Gwan; Schlessinger, Joseph; Rhee, Sue Goo

doi:10.1016/0092-8674(91)90461-7

Cited by 551 publications

(332 citation statements)

References 29 publications

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“…PLC-g1 activation is induced upon its binding to specific phosphotyrosine residues in activated RTKs or to adaptor proteins (Rhee et al, 2000). As a consequence, PLC-g1 itself becomes phosphorylated on tyrosine residues 771, 738 and 1254, with the last two sites correlating with stimulation of its enzymatic activity (Kim et al, 1990(Kim et al, , 1991.…”

Section: Discussionmentioning

confidence: 99%

Novel pathway in Bcr-Abl signal transduction involves Akt-independent, PLC-γ1-driven activation of mTOR/p70S6-kinase pathway

Markova¹,

Albers

Breitenbuecher

et al. 2009

Oncogene

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Section: Discussionmentioning

confidence: 99%

Novel pathway in Bcr-Abl signal transduction involves Akt-independent, PLC-γ1-driven activation of mTOR/p70S6-kinase pathway

Markova¹,

Albers

Breitenbuecher

et al. 2009

Oncogene

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“…The role of other tyrosines is less clear. Data from Kim et al (14) suggested that after PDGF receptor (PDGFR) stimulation, mutation of Y1254 inhibited, and mutation of Y771 enhanced PLC␥1 activity. Recent work from this group, however, raises questions about the significance of Y771 and Y1254 phosphorylation in terms of PLC␥1 activity after both AgR and PDGFR stimulation (23).…”

Section: Y775 and Y783 Phosphorylation Is Required For Plc␥1-dependenmentioning

confidence: 99%

“…PLC␥1 Y783, and its counterpart Y759 in PLC␥2, has been shown by several groups to be important for receptor-mediated activation of PLC␥1 (14,19,20,22,23). The role of other tyrosines is less clear.…”

Section: Y775 and Y783 Phosphorylation Is Required For Plc␥1-dependenmentioning

confidence: 99%

“…The tyrosine phosphorylation sites on PLC␥1 were characterized by phosphopeptide mapping and sequencing (10,11) and PLC␥1 Y771 and Y783 were suggested as the homologues to PLC␥2 Y753 and Y759 (14,19,22,23). Upon reassessment of the sequences, we proposed that PLC␥1 Y775 rather than PLC␥1 Y771 was the more likely equivalent for PLC␥2 Y753 ( Fig.…”

Section: Tyrosine 775 Of Plc␥1 Is Phosphorylated Upon Tcr and Bcr Actmentioning

confidence: 99%

“…In addition, early studies indicated Y1254 was needed for maximal growth factor-induced stimulation, while Y771 was proposed as a negative regulator. However, in later studies, the role of these two tyrosines has been questioned (14).…”

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confidence: 99%

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A New Tyrosine Phosphorylation Site in PLCγ1: The Role of Tyrosine 775 in Immune Receptor Signaling

Serrano

Graham

DeBell

et al. 2005

The Journal of Immunology

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Phospholipase Cγ (PLCγ) is a ubiquitous gatekeeper of calcium mobilization and diacylglycerol-mediated events induced by the activation of Ag and growth factor receptors. The activity of PLCγ is regulated through its controlled membrane translocation and tyrosine (Y) phosphorylation. Four activation-induced tyrosine phosphorylation sites have been previously described (Y472, Y771, Y783, and Y1254), but their specific roles in Ag receptor-induced PLCγ1 activation are not fully elucidated. Unexpectedly, we found that the phosphorylation of a PLCγ1 construct with all four sites mutated to phenylalanine was comparable with that observed with wild-type PLCγ1, suggesting the existence of an unidentified site(s). Sequence alignment with known phosphorylation sites in PLCγ2 indicated homology of PLCγ1 tyrosine residue 775 (Y775) with PLCγ2 Y753, a characterized phosphorylation site. Tyrosine 775 was characterized as a phosphorylation site using phospho-specific anti-Y775 antiserum, and by mutational analysis. Phosphorylation of Y775 did not depend on the other tyrosines, and point mutation of PLCγ1 Y775, or the previously described Y783, substantially reduced AgR-induced calcium, NF-AT, and AP-1 activation. Mutation of Y472, Y771, and Y1254 had no effect on overall PLCγ1 phosphorylation or activation. Although the concomitant mutation of Y775 and Y783 abolished downstream PLCγ1 signaling, these two tyrosines were sufficient to reconstitute the wild-type response in the absence of functional Y472, Y771, and Y1254. These data establish Y775 as a critical phosphorylation site for PLCγ1 activation and confirm the functional importance of Y783.

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Early human T cell activation events with engagement of surface MHC class II

King

Nguyen

1998

J. Cell. Biochem.

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Major histocompatibility complex (MHC) class II are expressed on most activated human lymphocytes. They direct antigen presentation events in dendritic cells and B cells (collectively called antigen presenting cells), but the role for MHC class II in human T cells is not well understood. To understand the role of surface MHC class II and to identify the molecules involved in signaling, we have defined the early activation sequence in T cells when MHC class II are engaged by a specific antibody. Specifically, we have characterized the involvement of phosphotyrosine kinases, phospholipase C (PLC), and Ca2+ mobilization. With the engagement by either whole anti-class II antibody or its Fab fragments, the enzymatic activity of p56lck and ZAP-70 increased, but there was no increase in p59fyn activity. In addition, the intracellular free Ca2+ increased, which was due to enhanced influx and not to the mobilization of intracytoplasmic Ca2+. These events did not require cross-linking because they were not significantly augmented by the addition of antispecies antibody. The coimmunoprecipitation of tyrosine phosphorylated PLC-gamma1 with surface MHC class II suggested that PLC-gamma1 could be recruited to MHC class II after engagement. These results show the complexities of the early signals transduced by the engagement of surface MHC class II on T cells.

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PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254

Cited by 551 publications

References 29 publications

Novel pathway in Bcr-Abl signal transduction involves Akt-independent, PLC-γ1-driven activation of mTOR/p70S6-kinase pathway

Novel pathway in Bcr-Abl signal transduction involves Akt-independent, PLC-γ1-driven activation of mTOR/p70S6-kinase pathway

A New Tyrosine Phosphorylation Site in PLCγ1: The Role of Tyrosine 775 in Immune Receptor Signaling

Early human T cell activation events with engagement of surface MHC class II

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