The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor.

Donovan, Jerald A.; Wange, Ronald L.; Langdon, Wallace Y.; Samelson, Lawrence E.

doi:10.1016/s0021-9258(17)31595-8

Cited by 284 publications

(36 citation statements)

References 33 publications

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“…Neverthe les s, recent studies have shown tyrosIn. e phosphory lation of p120 c -cbl in resp onse to T cell-receptor activation as well (21). Th us, p120c-cbl emerges as an important play er in imm un e recognition receptor signaling in hematopoietic cells.…”

Section: Discussionmentioning

confidence: 99%

Identification of the Major Tyrosine Kinase Substrate in Signaling Complexes Formed after Engagement of Fcγ Receptors

Marcilla¹,

Rivero-Lezcano

Agarwal

et al. 1995

Journal of Biological Chemistry

115

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We have recently identified the protein product of the c-cbl proto-oncogene as an SH3 binding protein expressed in macrophages. To investigate the possibility that p120c-cbl is involved in signaling pathways initiated by cell surface receptors for IgG (Fc gamma R), lysates of HL60 cells were examined for tyrosine phosphorylation of p120c-cbl upon Fc gamma R engagement. Our findings demonstrate that p120c-cbl is tyrosine-phosphorylated upon Fc gamma R engagement and that this molecule represents the major tyrosine kinase substrate in this signaling pathway. Protein complexes containing p120c-cbl, p72syk, and p56lyn were observed either in resting or activated cells. In vitro studies showed that the direct association between p120c-cbl and p56lyn was mediated by the SH3 domain of p56lyn.

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Section: Discussionmentioning

confidence: 99%

Identification of the Major Tyrosine Kinase Substrate in Signaling Complexes Formed after Engagement of Fcγ Receptors

Marcilla¹,

Rivero-Lezcano

Agarwal

et al. 1995

Journal of Biological Chemistry

115

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“…The GST moiety alone was expressed from a pGEX-KG vector without any insert (16). The GST-cyclin B, GST-furin , and GST-Grb2 expression plasmid s were constructed as described elsewhere (17)(18)(19). GST a nd all of th e GST fusion protein s were expresse d and prepar ed as described previously (15).…”

Section: Methodsmentioning

confidence: 99%

The RCC1 Protein Interacts with Ran, RanBP1, hsc70, and a 340-kDa Protein in Xenopus Extracts

Saitoh

Dasso

1995

Journal of Biological Chemistry

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RCC1 is an abundant, highly conserved, chromatin-associated protein whose function is necessary for the preservation of a properly ordered cell cycle. RCC1 is also necessary for numerous nuclear processes, including nuclear transport and RNA metabolism; and it functions enzymatically as a guanine nucleotide exchange factor for a small, ras-related GTPase called Ran. Studies in several organisms suggest that RCC1 may be part of a large complex containing multiple proteins. There is also evidence that RCC1 associates with chromatin through other proteins and that the binding of the complex to chromatin varies within the cell cycle. In order to characterize this putative complex, we have identified a number of other proteins as candidate components of the complex by their association with a GST-RCC1 fusion protein. Three of these proteins have previously been identified (Ran, RanBP1, and hsc70). The fourth protein is novel and has a molecular mass of 340 kDa. In this report, we discuss a preliminary characterization of the interactions between these proteins.

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“…ZAP-70 is subsequently tyrosinephosphorylated by p56 lck , which leads to the upregulation of ZAP-70 kinase activity [10,11]. Activated Src-family tyrosine kinases and ZAP-70 tyrosine kinases phosphorylate downstream substrates, such as phospholipase Cγ1 (PLCγ1) [12], the proto-oncogene Vav [13], Cbl [14], SLP-76 [15], and LAT (linker for activation of T cells) [16][17][18][19], thereby initiating signaling cascades that culminate in the activation of cytokine gene transcription through the activation of transcription factors such as nuclear factor of activated T cells (NFAT) [1][2][3][4].…”

Section: Introductionmentioning

confidence: 99%

The hematopoietic-specific adaptor protein Gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors

et al. 1999

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The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor.

Cited by 284 publications

References 33 publications

Identification of the Major Tyrosine Kinase Substrate in Signaling Complexes Formed after Engagement of Fcγ Receptors

Identification of the Major Tyrosine Kinase Substrate in Signaling Complexes Formed after Engagement of Fcγ Receptors

The RCC1 Protein Interacts with Ran, RanBP1, hsc70, and a 340-kDa Protein in Xenopus Extracts

The hematopoietic-specific adaptor protein Gads functions in T-cell signaling via interactions with the SLP-76 and LAT adaptors

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