SH2 domains, interaction modules and cellular wiring

Pawson, Tony; Gish, Gerald; Nash, Piers

doi:10.1016/s0962-8924(01)02154-7

Cited by 359 publications

(294 citation statements)

References 80 publications

Supporting

Mentioning

292

Contrasting

Unclassified

Order By: Relevance

“…The three ALKamplified neuroblastoma cell lines showed constitutive activation of full-length ALK and the increased local concentration of receptor tyrosine kinases appeared to interfere with signals from other RTKs. It is possible that ALK-ShcC signal activation has additional effects on the malignant tumor progression of neuroblastoma, probably similar to the mechanism reported in EGFR and Neu/ErbB2 (Andrechek et al, 2000;Pawson et al, 2001).…”

Section: Introductionmentioning

confidence: 56%

Domain-specific function of ShcC docking protein in neuroblastoma cells

Miyake

Hakomori²,

Misu

et al. 2005

Oncogene

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 56%

Domain-specific function of ShcC docking protein in neuroblastoma cells

Miyake

Hakomori²,

Misu

et al. 2005

Oncogene

View full text Add to dashboard Cite

“…SH2 domains are highly abundant in animal cells as adaptor modules that connect proteins in tyrosine kinase pathways, and are important mediators in cellular signaling. 14,15 Structural information is available for SH2 domains and their complexes with phosphopeptides, including that of the Src SH2 domain-phosphopeptide complex. 16 SH2 domains can be divided into two structural subfamilies: the Src-type and the STATtype subfamilies.…”

Section: Introductionmentioning

confidence: 99%

Structure and in Vivo Requirement of the Yeast Spt6 SH2 Domain

Dengl

Mayer

Sun

et al. 2009

Journal of Molecular Biology

View full text Add to dashboard Cite

During transcription elongation through chromatin, the Ser2-phosphorylated C-terminal repeat domain of RNA polymerase II binds the C-terminal Src homology 2 (SH2) domain of the nucleosome re-assembly factor Spt6. This SH2 domain is unusual in its specificity to bind phosphoserine, rather than phosphotyrosine and because it is the only SH2 domain in the yeast genome. Here, we report the high-resolution crystal structure of the SH2 domain from Candida glabrata Spt6. The structure combines features from both structural subfamilies of SH2 domains, suggesting it resembles a common ancestor of all SH2 domains. Two conserved surface pockets deviate from those of canonical SH2 domains, and may explain the unusual phosphoserine specificity. Differential gene expression analysis reveals that the SH2 domain is required for normal expression of a subset of yeast genes, and is consistent with multiple functions of Spt6 in chromatin transcription.

show abstract

“…Shc proteins are composed of an N-terminal phosphotyrosine binding (PTB) domain, a central glycine/prolinerich region (CH1) and a C-terminal Src homology 2 (SH2) domain (Pelicci et al, 1992;van der Geer et al, 1995). The binding affinity of the PTB domain and the SH2 domain to phosphotyrosine residues of RTKs transfers Shc proteins toward the cellular membrane upon ligand stimulation (Laminet et al, 1996;Pawson et al, 2001;van der Geer et al, 1996). Shc proteins phosphorylated at tyrosine residues by activated RTKs subsequently recruit SH2-containing adaptor molecules such as Grb2 (Gotoh et al, 1996;van der Geer et al, 1996).…”

Section: Introductionmentioning

confidence: 99%