anti-SH3-Domain Kinase Binding Protein 1 (SH3KBP1) Antikörper

Human SH3-Domain Kinase Binding Protein 1 (SH3KBP1) Interaktionspartner

1. These studies demonstrate a requirement for human herpesvirus 5 pUL135 interactions with Abi-1 and CIN85 for regulation of EGFR and mechanistically link the regulation of EGFR to virus reactivation.

2. Transcriptional regulation of NOX genes expression in human breast adenocarcinoma cells is modulated by adaptor protein CIN85.

3. The multiple Src homology 3 (SH3) domains of trimeric CIN85 molecules associated with multiple SLP-65 molecules, which recruited further CIN85 trimers, thereby perpetuating the oligomerization process.

4. these data support a role for the novel PP2Ac-CIN85 complex in supporting integrin-dependent platelet function by dampening the phosphatase activity.

5. CIN85 promotes recycling of TGF-beta receptors and thereby positively regulates TGF-beta signaling.

6. we demonstrate that SEPT9 negatively regulates EGFR degradation by preventing the association of the ubiquitin ligase Cbl with CIN85, resulting in reduced EGFR ubiquitylation

7. Results support the model that Cbl-CIN85-endophilin complex is not required for efficient internalization of EGFR, a prototype RTK.

8. Multiple molecular forms of adaptor protein Ruk/CIN85 specifically associate with different subcellular compartments in human breast adenocarcinoma cell line.

9. LOX-PP interacts with CIN85 via a novel SH3-binding motif and this association reduces CIN85-promoted invasion by breast cancer cells.

10. an FRS2beta-CIN85/CD2AP-Cbl axis for downregulation of ErbB2 may regulate ErbB2 protein levels in physiological and pathological settings

11. Data show that EGFR activation leads to a pronounced src-mediated tyrosine phosphorylation of CIN85 that subsequently influences EGFR ubiquitination.

12. this study indicates that high levels of Ruk(l)/CIN85 contribute to the conversion of breast adenocarcinoma cells into a more malignant phenotype via modulation of the Src/Akt pathway.

13. Data show that CIN85 (c-Cbl interacting protein of 85 kDa) is constitutively associated with c-Cbl, Cbl-b, and B-cell linker in B cells.

14. Live cell imaging and co-immunoprecipitation experiments confirmed that both SLP65 and CIN85 are both required for the onset and progression phases of B-cell antigen receptor signal transduction.

15. The CIN85 was constitutively associated with Hrs, and this strengthens the hypothesis of a functional role of CIN85 in endosomal EGFR sorting.

16. the ubiquitination and degradation of stimulated FcgammaRIIa mediated by c-Cbl are positively regulated by the adaptor protein CIN85 in a PKC-dependent manner and these events contribute to the termination of FcgammaRIIa signaling.

17. the N- and C-termini are important for the structure, stability, and function of the third SH3 domain of CIN85

18. ARAP1 associated with CIN85 affects epidermal growth factor receptor endocytic trafficking.

19. High CIN85 is associated with the development and progression of head and neck squamous cell carcinoma.

20. CIN85 binding to a C-terminal motif within hTTP leads to the increased phosphorylation of hTTP, possibly through enhanced association with MEKK4

Mouse (Murine) SH3-Domain Kinase Binding Protein 1 (SH3KBP1) Interaktionspartner

1. Cin85-deficient mother mice had reduced pituitary hormone prolactin secretion as a result of excessive dopamine signaling in the brain. Their offspring matured normally and produced their own pups; however, nurturing behaviors such as pup retrieval and nursing were strongly inhibited.

2. competitive analytical gel-filtration chromatography and isothermal titration calorimetry (ITC) results showed that ARAP1 could compete with Cbl for CIN85 binding, which provides a biochemical basis for the regulatory roles of ARAP1 in the CIN85-mediated EGFR internalizing process.

3. CIN85/RukL is involved in endocytosis of nephrin in podocytes under diabetic conditions, causing podocyte depletion and promoting proteinuria. CIN85/RukL expression therefore shows potential to be a novel target for antiproteinuric therapy in diabetes.

4. Dab1 mediated the association of CIN85 with ApoER2 or VLDLR in neurons.

5. Data suggest that Ser587 Cin85 phosphomimetic mutant protein shows dramatically reduced binding to Dab1 (disabled protein 1) (without affecting binding to CapZ).

6. Sh3kbp1 is SUMOylated by SUMO-1, -2, and -3 and that SUMOylation is enhanced in the presence of Cd2ap.

7. the interaction between SHIP-1 and CIN85 might synergistically facilitate the down-regulation of phosphatidylinositol-3,4,5-trisphosphate levels.

8. Live cell imaging and co-immunoprecipitation experiments confirmed that both SLP65 and CIN85 are both required for the onset and progression phases of B-cell antigen receptor signal transduction.

9. a B cell-specific deletion of CIN85 led to impaired T cell-independent type II antibody responses in vivo and diminished IKK-beta activation and cellular responses to B cell receptor cross-linking in vitro

10. Coexpression of CIN85/Ruk(L) with CD2AP led to a decreased binding of CIN85/Ruk(L) to nephrin and podocin, which indicates a functional competition between CD2AP and CIN85/Ruk(L).

11. Data indicate an important function of CIN85 (SH3KBP1) in the regulation of dopamine D2 receptor functions and provide a molecular explanation for the hyperactive behaviour of CIN85(Deltaex2) mice.

12. CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases

13. Analysis of cDNA clones, ESTs and products of RT-PCR amplifications with different combinations of primers revealed how alternative splicing and promoter usage generate a variety of Ruk transcripts and encoded protein isoforms in different mouse tissues.

14. role of CD2AP/CIN85 protein balance in the normal signaling response of podocytes.

15. Therefore, CIN85 might play different roles in the dopaminergic cell line and in the

16. SH3-domain kinase binding protein 1 may function as a scaffold molecule in both the internalization and endocytic cargo sorting processes through its association with the endosomal membrane.