Proteins recruited by SH3 domains of Ruk/CIN85 adaptor identified by LC-MS/MS

Havrylov, Serhiy; Rzhepetskyy, Yuriy; Malinowska, Agata; Drobot, L. B.; Redowicz, Maria Jolanta

doi:10.1186/1477-5956-7-21

Cited by 47 publications

(53 citation statements)

References 92 publications

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“…This emphasizes the importance of CBL-associated deregulation of signaling in chronic myeloid diseases and constitutes an incentive to look for alterations in other members of the CBL/CIN85 pathway. 12 In that respect we found a gain of the gene encoding MAP3K4, an interactor of CIN85, 13 in a RAEB1 with complex aCGH profile, and a gain of the gene encoding the CBL interactor ARHGEF7/bPIX in an RCMD in a reported study. 14 Whether other E3 ubiquitin ligases (for example, AHR or SCF components) may have a role in these diseases also needs to be investigated.…”

mentioning

confidence: 54%

Gain of CBL-interacting protein, a possible alternative to CBL mutations in myeloid malignancies

et al. 2010

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mentioning

confidence: 54%

Gain of CBL-interacting protein, a possible alternative to CBL mutations in myeloid malignancies

et al. 2010

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“…on May 11, 2018. by guest www.bloodjournal.org From function of coated vesicles. 25 Similarly, early studies showed a characteristic feature of CIN85 in the formation of clathrin-coated vesicles during the internalization of RTKs such as EGFRs in nonimmune cells. 18,19 Brain-specific CIN85-deficient mice manifest impaired internalization of D2 dopamine receptors, which belong to the 7-transmembrane G protein-coupled receptor superfamily.…”

Section: Discussionmentioning

confidence: 93%

“…1,2 Because SH3 domains play an important role in the function of CIN85, 25 we focused on For personal use only. on May 11, 2018. by guest www.bloodjournal.org From tyrosine-phosphorylated molecules downstream of the BCR that could associate with the SH3 domains of CIN85.…”

Section: Cin85 Associates With Cbl and Blnk And Regulates Their Phospmentioning

confidence: 99%

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CIN85 is required for Cbl-mediated regulation of antigen receptor signaling in human B cells

Niiro

Jabbarzadeh-Tabrizi

Kikushige

et al. 2012

Blood

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IntroductionB-cell receptor (BCR) signaling guides critical cell fate decisions in B cells during ontogeny. 1,2 BCRs can generate tolerogenic signals to purge or silence B cells that bind to self-antigens, and immunogenic signals to expand B cells that are specific for foreign antigens. Thus, BCR signaling must be properly regulated at the various stages of B-cell development, as aberrant regulation of BCR signaling potentially leads to autoimmunity and B-cell malignancies.On BCR ligation by antigens, the Src-family protein tyrosine kinase (PTK) Lyn and Syk are initially activated. Syk propagates the signal by phosphorylating downstream signaling molecules, causing the activation of critical signaling intermediates phosphoinositol 3-kinase (PI3K) and phospholipase C (PLC)␥2. PI3K activates Akt kinase, which is important for B-cell survival. 3 PLC␥2 activation induces the release of intracellular Ca 2ϩ and the activation of protein kinase C (PKC), which cause the activation of mitogen-activated protein kinases (MAPKs; ERK, JNK, and p38 MAPK) and of transcription factors, including NF-B and NF-AT. These molecules regulate further downstream molecules that are responsible for determining B-cell fates such as survival, growth, and differentiation. 1,2 Casitas B-lineage lymphoma (Cbl) proteins are E3 ubiquitin ligases that regulate signals of various receptors by promoting the ubiquitination of signaling components. 4,5 Tyrosine phosphorylation of Cbl proteins is critical for their function. 6 Mammalian Cbl proteins consist of 3 members, c-Cbl, Cbl-b, and Cbl-3, among which c-Cbl and Cbl-b are expressed in hematopoietic cells. 7 In B cells, Cbl proteins associate with Syk and B-cell linker (BLNK), and negatively regulate BCR signaling. 8,9 B cell-specific ablation of c-Cbl/Cbl-b proteins in mice causes aberrant BCR signaling as well as impaired B-cell anergy, culminating in the development of systemic lupus erythematosus (SLE)-like disease. 10 In addition, c-Cbl is hypophosphorylated on tyrosine in advanced stages of chronic lymphocytic leukemia (CLL). 11 These findings suggest that Cbl-mediated regulation of BCR signaling is critical for the fate decisions of self-reactive and malignant B cells.Adaptors are noncatalytic molecules that integrate the spatial and temporal assembly of multiprotein complexes involved in the survival, growth, and differentiation of B cells. We previously showed that the B lymphocyte adaptor molecule of 32 kDa (Bam32)/DAPP1 regulates BCR signaling/internalization and B-cell survival. 12,13 The SH3KBP1 (SH3-domain kinase-binding protein 1) gene, which is also known as CIN85 (c-Cbl interacting protein of 85 kDa), encodes an adaptor that is independently identified by several groups and contains 3 SH3 domains, a proline-rich region, and a coiled-coil domain. [14][15][16][17] Early studies showed that in nonimmune cells, CIN85 regulates the clathrindependent internalization of receptor tyrosine kinases (RTKs) such as epidermal growth factor receptors (EGFRs). 18,19 The formation of the ternary...

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“…Insights & Perspectives ..... PDGFR [28] p130Cas [70] Vinexin [76] PR130 [47] FcgRIIB [64] p85a [62] Filamin [77] SHIP1 [82] FcgRIIA [65] APS [71] Actin [77] M-CSFR [66] DOK-1 [72] Intersectin1 [78] cMET [67] JIP-1 [73] ARAP-3 [79] ABL [62] CD2AP [74] CIN-85 [80] EphrinA2R [68] SH3YL1 [54] Lamin A/C [22] JIP-1, JNK-interacting protein 1; PTP1B, protein-tyrosine phosphatase 1B; CD2AP, CD2-associated protein; SH3YL1, SH3 domain-containing Ysc84-like 1; PDGFR, platelet-derived growth factor receptor; EGFR, epidermal growth factor receptor; M-CSFR, macrophage colony-stimulating factor receptor; cMET, hepatocyte growth factor (HGF/SF) receptor; EphrinA2R, ephrinA2 receptor; ARAP-3, Arf GAP, Rho GAP, ankyrin repeat and PH domains. It is proposed that SHIP2 is phosphorylated to phospho SHIP2 (pSHIP2) S132 in the cytoplasm.…”

Section: W Elong Edimo Et Almentioning

confidence: 99%

Reversible Ser/Thr SHIP phosphorylation: A new paradigm in phosphoinositide signalling?

et al. 2012

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Phosphoinositide (PI) phosphatases such as the SH2 domain-containing inositol 5-phosphatases 1/2 (SHIP1 and 2) are important signalling enzymes in human physiopathology. SHIP1/2 interact with a large number of immune and growth factor receptors. Tyrosine phosphorylation of SHIP1/2 has been considered to be the determining regulatory modification. However, here we present a hypothesis, based on recent key publications, highlighting the determining role of Ser/Thr phosphorylation in regulating several key properties of SHIP1/2. Since a subunit of the Ser/Thr phosphatase PP2A has been shown to interact with SHIP2, a putative mechanism for reversing SHIP2 Ser/Thr phosphorylation can be anticipated. PI phosphatases are potential target molecules in human diseases, particularly, but not exclusively, in cancer and diabetes. Therefore, this novel regulatory mechanism deserves further attention in the hunt for discovering novel or complementary therapeutic strategies. This mechanism may be more broadly involved in regulating PI signalling in the case of synaptojanin1 or the phosphatase, tensin homolog, deleted on chromosome TEN.

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Proteins recruited by SH3 domains of Ruk/CIN85 adaptor identified by LC-MS/MS

Cited by 47 publications

References 92 publications

Gain of CBL-interacting protein, a possible alternative to CBL mutations in myeloid malignancies

Gain of CBL-interacting protein, a possible alternative to CBL mutations in myeloid malignancies

CIN85 is required for Cbl-mediated regulation of antigen receptor signaling in human B cells

Reversible Ser/Thr SHIP phosphorylation: A new paradigm in phosphoinositide signalling?

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