Elucidation of the biological function of phosphotyrosine adaptor Shc A.
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Elucidation of the biological function of phosphotyrosine adaptor Shc A. by Ka-Man Venus Lai

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Published .
Written in English

Book details:

The Physical Object
Pagination206 leaves.
Number of Pages206
ID Numbers
Open LibraryOL19081820M
ISBN 100612690598

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The MAPK isoform ERK2 [71], the adaptor protein Shc [74] and Ras [56] have been localized in human sperm head indicating that this pathway may be required for regulating protein phosphorylation in. Specificity in Signal Transduction: From Phosphotyrosine-SH2 Domain Interactions to Complex Cellular Systems SH2 or phosphotyrosine (pY) binding domains, Shc, importance in cellular Author: Tony Pawson. Tyrosine phosphorylation plays a role in virtually every step in the development and function of a neuron, including survival and differentiation, the extension of axons to their targets and synapse formation and function (Fig. ). Due to the large number of topics involved, the following is by no means a complete account of all of the functions of tyrosine phosphorylation in the nervous Author: Lit-fui Lau, Richard L Huganir. Nck: The potential role of the adaptor protein Nck in FGF function remains to be established, but in a recent report, Nck was shown to participate in FGFR-1 signal transduction during mesoderm induction in Xenopus (77). The Nck SH2 domain binds to the same phosphotyrosine-containing motif as Crk, and therefore, Y is a potential binding site.

In some cases, GRB2 binds directly to phosphotyrosine residues on the cytoplasmic tail of the receptor via its SH2 domain. Alternatively, SHC can bind first and then recruit GRB2. In addition to an SH2 domain, GRB2 has two SH3 domains that bind proline-rich segments of the guanine nucleotide exchange factor son of sevenless protein (SOS. Abstract. The elucidation of intracytoplasmic signaling pathways is a ctriical step in the precise understanding of cell biology. In this regard, the identification of intracytoplasmic domains, which are specialized in the transmission of biological messages, has been an enormous breakthrough ().Among these transducing domains, the src homology 2 (SH2) domains are specialized in the Cited by: This book consists of a series of reviews on selected topics within the rapidly and vastly expanding field of membrane biology. Its aim is to highlight the most significant and important advances that have been made in recent years in understanding the structure, dynamics and functions of cell membranes. Background. Fibroblast growth factors (FGFs) constitute a family of structurally related proteins, which regulate many facets of cell behaviour, from embryonic patterning, to tissue repair and metabolism [].FGFs exert their effects on cells by interacting with a signalling receptor tyrosine kinase (FGFR) and a glycosaminoglycan co-receptor, usually heparan sulfate (HS) [].Cited by:

If the address matches an existing account you will receive an email with instructions to retrieve your username. Starting with an overview of cell signalling and highlighting its importance in many biological systems, the book goes on to explore the key components of extracellular and intracellular signalling mechanisms before examining how these components come together to create signalling pathways, which are so crucial to the survival of many living. In addition to Gab1, the Grb2 and Shc adaptor proteins are critical mediators of MET activation. Grb2 and Shc associate with MET and other RTKs through their respective SH2 and PTB domains (Furge et al. ). Grb2 is able to directly bind to MET through its SH2 and SH3 domains, but is also recruited indirectly through by:   The fibroblast growth factor receptor (FGFR) interprets concentration gradients of FGF ligands and structural changes in the heparan sulfate (HS) co-receptor to generate different cellular responses. However, whether the FGFR generates different signals is not known. We have previously shown in rat mammary fibroblasts that in cells deficient in sulfation, and so in HS co-receptor, FGF-2 Cited by: