Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins.

Ron, Dorit; Chen, Che‐Hong; Caldwell, Jeremy; Jamieson, Lee; Orr, Elisha; Mochly‐Rosen, Daria

doi:10.1073/pnas.91.3.839

Cited by 678 publications

(668 citation statements)

References 34 publications

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“…Spatial and temporal control of PKC signalling is also influenced via interaction with adaptor/scaffolding proteins that anchor the PKCs to various intracellular locations in the cell. A multitude of adaptor proteins that influence PKC function have been characterised, including A-Kinase Anchoring Proteins (AKAPs) [15,16], Receptors for Activated C Kinases (RACKs) [17,18] and 14-3-3 proteins [19,20]. Termination of PKC signalling is best described for cPKCs and nPKCs.…”

Section: Accepted M Manuscriptmentioning

confidence: 99%

Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites

Freeley

Kelleher

Long

2011

Cellular Signalling

105

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Section: Accepted M Manuscriptmentioning

confidence: 99%

Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites

Freeley

Kelleher

Long

2011

Cellular Signalling

105

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“…The analysis yielded several putative binding partners (Supplementary Table 1), one of these being RACK1 (Ron et al, 1994; Figure 6a). In an independent experiment, we quantified the relative amounts of RACK1 in Copine-III IPs from SKBr3 lysates by MRM.…”

Section: Copine-iii Interacts With Rack1 and Both Proteins Complex Wimentioning

confidence: 99%

Copine-III interacts with ErbB2 and promotes tumor cell migration

et al. 2009

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ErbB2 amplification and overexpression in breast cancer correlates with aggressive disease and poor prognosis. To find novel ErbB2-interacting proteins, we used stable isotope labeling of amino acids in cell culture followed by peptide affinity pull-downs and identified specific binders using relative quantification by mass spectrometry. Copine-III, a member of a Ca 2 þ -dependent phospholipid-binding protein family, was identified as binding to phosphorylated Tyr1248 of ErbB2. In breast cancer cells, Copine-III requires Ca 2 þ for binding to the plasma membrane, where it interacts with ErbB2 upon receptor stimulation, an interaction that is dependent on receptor activity. Copine-III also binds receptor of activated C kinase 1 and colocalizes with phosphorylated focal adhesion kinase at the leading edge of migrating cells. Importantly, knockdown of Copine-III in T47D breast cancer cells causes a decrease in Src kinase activation and ErbB2-dependent wound healing. Our data suggest that Copine-III is a novel player in the regulation of ErbB2-dependent cancer cell motility. In primary breast tumors, high CPNE3 RNA levels significantly correlate with ERBB2 amplification. Moreover, in an in situ tissue microarray analysis, we detected differential protein expression of Copine-III in normal versus breast, prostate and ovarian tumors, suggesting a more general role for Copine-III in carcinogenesis.

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“…Previous studies have shown RACK1 to be expressed in a variety of cells including rat brain (Ron et al, 1994;Pascale et al, 1996), rat kidney (Padanilam and Hammerman, 1997) and a number of cell lines (Cloud-He¯in et al, 1996). However, thus far RACK1 expression in leukocytes has not been demonstrated.…”

mentioning

confidence: 99%

“…Identi®ed as a receptor for activated protein kinase C (PKC; Ron et al, 1994), RACK1 is believed to interact with speci®c sites in the C2 region of PKC in the presence of PKC activators (Ron et al, 1995a), causing stabilization of the active form of the enzyme (Ron et al, 1995b). To con®rm the interaction between bc and RACK1, we determined whether the Figure 1 RACK-1 interacts speci®cally with the IL-5/IL-3/GM-CSF receptor bc.…”

mentioning

confidence: 99%

“…We did not ®nd any homology between the cytoplasmic domain of bc and the membrane proximal RACK1-binding domain of the integrin b 1 ± 2 subunit, suggesting that di erent regions of RACK1 may associate with bc and the integrin b 1 ± 2 subunit. RACK1 has previously been described to bind activated PKCb (Ron et al, 1994). Several groups have shown that overexpression of PKC mimicks some aspects of IL-5/IL-3/GM-CSF signalling such as proliferation and di erentiation of haematopoietic precursor cells (Pierce et al, 1998;Gubina et al, 1998;Rossi et al, 1996).…”

mentioning

confidence: 99%

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Association of RACK1 and PKCβ with the common β-chain of the IL-5/IL-3/GM-CSF receptor

Geijsen¹,

Spaargaren

Raaijmakers³

et al. 1999

Oncogene

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Granulocyte macrophage colony stimulating factor (GM-CSF), interleukin-3 (IL-3) and interleukin-5 (IL-5 belong to a family of cytokines that regulate proliferation, di erentiation and function of haematopoietic cells. Their receptor consists of a ligand speci®c a-chain and a signal transducing b-chain (bc). While, the role of phosphotyrosine residues in the bc as mediators of downstream signalling cascades has been established, little is known about non-phosphotyrosine mediated events. To identify proteins interacting with bc, we screened a yeast two-hybrid library with the intracellular domain of bc. We found that RACK1, a molecule associating with activated PKC, PLCg and Src kinases, associated with the membrane proximal region of bc in both yeast two-hybrid, immunoprecipitation and GSTpull-down assays. The association of RACK1 was constitutive, demonstrating no alteration upon cellular stimulation. Furthermore, upon stimulation of cells with IL-5 or PMA, a complex of bc and PKCb was found. Together, these ®ndings suggest a novel role for RACK1 as a possible adapter molecule associating with the intracellular domain of cytokine receptors.

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Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins.

Abstract: Protein kinase C (PKC) translocates from the

Cited by 678 publications

References 34 publications

Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites

Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites

Copine-III interacts with ErbB2 and promotes tumor cell migration

Association of RACK1 and PKCβ with the common β-chain of the IL-5/IL-3/GM-CSF receptor

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