Acidic substitution of the activation loop tyrosines in TrkA supports nerve growth factor-independent cell survival and neuronal differentiation

Gryz, Ela A.; Meakin, Susan O.

doi:10.1038/sj.onc.1203330

Cited by 13 publications

(15 citation statements)

References 59 publications

(77 reference statements)

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“…However, the interaction may not occur at these phosphorylated tyrosine residues per se but rather may be a consequence of the conformational change the receptor undergoes upon activation. Having said this, however, the TrkA13 mutants are constitutively active; albeit this activity is reduced relative to wild type (27,55). The reduction in the level of activity observed in these TrkA13 mutants (27,55) suggests that, although these receptor mutants may assume an active conformation, it is probably less stable than that in the wild type receptor.…”

Section: Discussionmentioning

confidence: 99%

“…With respect to function, the TID1 proteins appear to play a fundamental role in both cell death and growth. For example, recessive mutations in TID56 bring about neoplastic transformation of imaginal disc cells resulting in larval death (53,54), and it has been shown that the TID1 isoforms function in both a proand antiapoptotic capacity (17,18 (27,55,56). Initially it was believed that these tyrosines do not participate as docking sites for signaling adapter proteins, but recently a number of proteins (APS, SH2B, and Grb2) have been reported to bind at these sites (13,14,57).…”

Section: Discussionmentioning

confidence: 99%

“…5A, have been described previously (10,14,27). The expression plasmids for wild type TrkB and TrkC were described before (10).…”

Section: Methodsmentioning

confidence: 99%

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Human Tumorous Imaginal Disc 1 (TID1) Associates with Trk Receptor Tyrosine Kinases and Regulates Neurite Outgrowth in nnr5-TrkA Cells

Liu

MacDonald

Hryciw

et al. 2005

Journal of Biological Chemistry

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The human tumorous imaginal disc 1 (TID1) proteins including TID1 L and TID1 S , members of the DnaJ domain protein family, are involved in multiple intracellular signaling pathways such as apoptosis induction, cell proliferation, and survival. Here we report that TID1 associates with the Trk receptor tyrosine kinases and regulates nerve growth factor (NGF)-induced neurite outgrowth in PC12-derived nnr5 cells. Binding assays and transfection studies showed that the carboxyl-terminal end of TID1 (residues 224 -429) bound to Trk at the activation loop (Tyr(P) 683 -Tyr 684 (P) 684 in rat TrkA) and that TID1 was tyrosine phosphorylated by Trk both in yeast and in transfected cells. Moreover endogenous TID1 was also tyrosine phosphorylated by and co-immunoprecipitated with Trk in neurotrophinstimulated primary rat hippocampal neurons. Overexpression studies showed that both TID1 L and TID1 S significantly facilitated NGF-induced neurite outgrowth in TrkA-expressing nnr5 cells possibly through a mechanism involving increased activation of mitogen-activated protein kinase. Consistently knockdown of endogenous TID1, mediated with specific short hairpin RNA, significantly reduced NGF-induced neurite growth in nnr5-TrkA cells. These data provide the first evidence that TID1 is a novel intracellular adaptor that interacts with the Trk receptor tyrosine kinases in an activity-dependent manner to facilitate Trk-dependent intracellular signaling.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Human Tumorous Imaginal Disc 1 (TID1) Associates with Trk Receptor Tyrosine Kinases and Regulates Neurite Outgrowth in nnr5-TrkA Cells

Liu

MacDonald

Hryciw

et al. 2005

Journal of Biological Chemistry

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“…NGF interacts with two entirely distinct groups of receptors (Rodrigueztebar et al, 1990;Frade and Barde, 1998): p75 neurotrophin receptor (p75NTR), a low-affinity receptor that has a similar affinity to each of the neurotrophins; and TrkA, a member of the Trk family of receptor tyrosine kinases, which binds selectively to NGF (Reichardt, 2006). NGF binding activates the kinase domain of TrkA, leading to autophosphorylation (Gryz and Meakin, 2000). The resulting phosphotyrosines become docking sites for adaptor proteins involved in signal transduction pathways that lead to the activation of Ras, Rac, phosphatidylinositol 3-kinase (PI3-K), phospholipase C-γ (PLC-γ) and other effectors (Kaplan and Miller, 2000;Huang and Reichardt, 2003).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure and functional implication of the RUN domain of human NESCA

et al. 2012

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“…NGF has two known receptors; TrkA, a single-pass transmembrane receptor-tyrosine kinase that binds selectively to NGF, and p75, a transmembrane glycoprotein that binds all members of the neurotrophin family (3,4). NGF binding activates the kinase domain of TrkA, leading to autophosphorylation (5). The resulting phosphotyrosines become docking sites for adaptor proteins involved in signal transduction pathways that lead to the activation of Ras, Rac, phosphatidylinositol 3-kinase, phospholipase C␥, and other effectors (2,6).…”

mentioning

confidence: 99%

Interaction of Mint2 with TrkA Is Involved in Regulation of Nerve Growth Factor-induced Neurite Outgrowth

Zhang

Wang

Zhang

et al. 2009

Journal of Biological Chemistry

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TrkA receptor signaling is essential for nerve growth factor (NGF)-induced survival and differentiation of sensory neurons. To identify possible effectors or regulators of TrkA signaling, yeast two-hybrid screening was performed using the intracellular domain of TrkA as bait. We identified muc18-1-interacting protein 2 (Mint2) as a novel TrkA-binding protein and found that the phosphotyrosine binding domain of Mint2 interacted with TrkA in a phosphorylation-and ligand-independent fashion. Coimmunoprecipitation assays showed that endogenous TrkA interacted with Mint2 in rat tissue homogenates, and immunohistochemical evidence revealed that Mint2 and TrkA colocalized in rat dorsal root ganglion neurons. Furthermore, Mint2 overexpression inhibited NGF-induced neurite outgrowth in both PC12 and cultured dorsal root ganglion neurons, whereas inhibition of Mint2 expression by RNA interference facilitated NGF-induced neurite outgrowth. Moreover, Mint2 was found to promote the retention of TrkA in the Golgi apparatus and inhibit its surface sorting. Taken together, our data provide evidence that Mint2 is a novel TrkA-regulating protein that affects NGF-induced neurite outgrowth, possibly through a mechanism involving retention of TrkA in the Golgi apparatus.

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Acidic substitution of the activation loop tyrosines in TrkA supports nerve growth factor-independent cell survival and neuronal differentiation

Cited by 13 publications

References 59 publications

Human Tumorous Imaginal Disc 1 (TID1) Associates with Trk Receptor Tyrosine Kinases and Regulates Neurite Outgrowth in nnr5-TrkA Cells

Human Tumorous Imaginal Disc 1 (TID1) Associates with Trk Receptor Tyrosine Kinases and Regulates Neurite Outgrowth in nnr5-TrkA Cells

Crystal structure and functional implication of the RUN domain of human NESCA

Interaction of Mint2 with TrkA Is Involved in Regulation of Nerve Growth Factor-induced Neurite Outgrowth

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