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NCK adaptor protein 1

Nck, Nck1
The protein encoded by this gene is one of the signaling and transforming proteins containing Src homology 2 and 3 (SH2 and SH3) domains. It is located in the cytoplasm and is an adaptor protein involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS. Alternatively spliced transcript variants encoding different isoforms have been found. [provided by RefSeq, Jun 2010] (from NCBI)
Top mentioned proteins: Actin, Src, CAN, V1a, Wasp
Papers using Nck antibodies
Deconvolution in optical microscopy
Galan Jorge, In PLoS Pathogens, 1996
... (a gift from Jack Taunton, USCF), anti-Arp2/3 (a gift from Matthew Welch, UC Berkeley), and anti-Nck (BD Biosciences Pharmingen) were used at ...
Papers on Nck
Identification of Phosphorylation Consensus Sequences and Endogenous Neuronal Substrates of the Psychiatric Risk Kinase TNIK.
Ehlers et al., Worcester, United States. In J Pharmacol Exp Ther, Feb 2016
Traf2- and Nck-interacting kinase (TNIK) is a serine/threonine kinase highly expressed in the brain and enriched in the postsynaptic density of glutamatergic synapses in the mammalian brain.
Integration of linear and dendritic actin nucleation in Nck-induced actin comets.
Mayer et al., San Martín, Argentina. In Mol Biol Cell, Feb 2016
The Nck adaptor protein recruits cytosolic effectors such as N-WASP that induce localized actin polymerization.
Nck Binds to the T Cell Antigen Receptor Using Its SH3.1 and SH2 Domains in a Cooperative Manner, Promoting TCR Functioning.
Pongcharoen et al., Phitsanulok, Thailand. In J Immunol, Feb 2016
It has been shown that the purified, recombinant SH3.1 domain of the adaptor molecule noncatalytic region of tyrosine kinase (Nck) can bind to the exposed PRS of CD3ε, but the molecular mechanism of how full-length Nck binds to the TCR in cells has not been investigated so far.
Nck influences preosteoblastic/osteoblastic migration and bone mass.
Ezura et al., Tokyo, Japan. In Proc Natl Acad Sci U S A, Jan 2016
Nck (noncatalytic region of tyrosine kinase; collectively referred to Nck1 and Nck2) is a member of the signaling adaptors that regulate cell migration and cytoskeletal structures, but its function in cells in the osteoblastic lineage is not known.
Targeting NCK-Mediated Endothelial Cell Front-Rear Polarity Inhibits Neo-Vascularization.
Eichmann et al., Paris, France. In Circulation, Jan 2016
The adaptor proteins Nck1 and 2 are known regulators of cytoskeletal dynamics and polarity, but their function in angiogenesis is poorly understood.
Therapeutic targets in the Wnt signaling pathway: Feasibility of targeting TNIK in colorectal cancer.
Yamada et al., Tokyo, Japan. In Pharmacol Ther, Dec 2015
Traf2- and Nck-interacting protein kinase (TNIK) has been identified as a regulatory component of the T-cell factor-4 and β-catenin transcriptional complex independently by two research groups.
Nck-mediated recruitment of BCAP to the BCR regulates the PI(3)K-Akt pathway in B cells.
Batista et al., London, United Kingdom. In Nat Immunol, 2013
The adaptor Nck links receptor signaling to cytoskeleton regulation.
Integration of signaling and cytoskeletal remodeling by Nck in directional cell migration.
Rivera et al., College Station, United States. In Bioarchitecture, 2013
Here we present an overview of how activation of the WASp/Arp2/3 pathway of actin remodeling by Nck coordinates directional cell migration and speculate on its role as a signaling integrator in the coordination of cellular processes involved in endothelial cell polarity and vascular lumen formation.
Roles of adaptor proteins in podocyte biology.
Ha, Ch'ŏngju, South Korea. In World J Nephrol, 2013
These adaptor proteins, such as CD2-associated protein, zonula occludens 1, β-catenin, Nck and p130Cas, located at the intracellular SD insertion area near lipid rafts, have important structural and functional roles.
A neuronal transmembrane protein LRFN4 complexes with 14-3-3s and NCK1 to induce morphological change in monocytic cells via Rac1-mediated actin cytoskeleton reorganization.
Kohroki et al., Noda, Japan. In Febs Lett, 2012
LRFN4 complexed with 14-3-3s and NCK1 to mediate elongation in monocytic cells via Rac-1-mediated actin cytoskeleton reorganization
c-ABL modulates MAP kinases activation downstream of VEGFR-2 signaling by direct phosphorylation of the adaptor proteins GRB2 and NCK1.
Galvagni et al., Siena, Italy. In Angiogenesis, 2012
the negative loop on p38 is mediated by c-ABL phosphorylation at tyrosine 105 of the adaptor protein NCK1, while the phosphorylation at tyrosine 209 of GRB2 down-modulates ERK1/2 and JNKs signaling.
Stoichiometry of Nck-dependent actin polymerization in living cells.
Mayer et al., Farmington, United States. In J Cell Biol, 2012
The results indicate that the density of Nck molecules in aggregates is a critical determinant of actin polymerization.
Studying the dynamics of SLP-76, Nck, and Vav1 multimolecular complex formation in live human cells with triple-color FRET.
Barda-Saad et al., Ramat Gan, Israel. In Sci Signal, 2012
both T cell activation and the association between SLP-76 and Nck. After T cell receptor stimulation, SLP-76 was phosphorylated, which enabled the binding of Nck.
Phase transitions in the assembly of multivalent signalling proteins.
Rosen et al., Dallas, United States. In Nature, 2012
In the case of the actin-regulatory protein called neural Wiskott-Aldrich syndrome protein (N-WASP) interacting with its established biological partners NCK and phosphorylated nephrin, the phase transition corresponds to a sharp increase in activity towards an actin nucleation factor, the Arp2/3 complex.
Essential role of the adaptor protein Nck1 in Jurkat T cell activation and function.
Pongcharoen et al., Phitsanulok, Thailand. In Clin Exp Immunol, 2012
Decreased Nck1 protein in Jurkat T cells resulted in an impairment of TCR-CD3-mediated activation involving a defective Erk phosphorylation pathway.
WIP remodeling actin behind the scenes: how WIP reshapes immune and other functions.
Barda-Saad et al., Ramat Gan, Israel. In Int J Mol Sci, 2011
Indeed, WIP was shown to interact with various binding partners, including the signaling proteins Nck, CrkL and cortactin.
[A uNick protein].
Larose et al., Montréal, Canada. In Med Sci (paris), 2011
Nck1 is an adaptor protein composed of 3 N-terminal SH3 domains followed by a unique Cterminal SH2 domain. It plays a role in cell migration, cell adhesion, actin polymerization, stress responses and cell survival. It is implicated in melanoma. Review.
The rate of N-WASP exchange limits the extent of ARP2/3-complex-dependent actin-based motility.
Way et al., London, United Kingdom. In Nature, 2009
Taking advantage of this, we have analysed the dynamics of neuronal Wiskott-Aldrich syndrome protein (N-WASP), WASP-interacting protein (WIP), GRB2 and NCK, which are required to stimulate actin-related protein (ARP)2/3-complex-dependent actin-based motility of vaccinia virus, using fluorescence recovery after photobleaching.
Connecting the dots between septins and the DNA damage checkpoint.
Takeda et al., Kyoto, Japan. In Cell, 2007
In this issue of Cell, Kremer et al. (2007) link septins to DNA damage in mammalian cells by identifying a new signaling pathway that includes the adaptors SOCS7 and NCK.
Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7.
Macara et al., Charlottesville, United States. In Cell, 2007
Demonstrate connection between septins/SOCS7/NCK signaling and the DNA damage response.
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