Epithelial Src homology region 2 domain–containing phosphatase‐1 restrains intestinal growth, secretory cell differentiation, and tumorigenesis

2017 ◽  
Vol 31 (8) ◽  
pp. 3512-3526 ◽  
Author(s):  
Caroline Leblanc ◽  
Marie‐Josée Langlois ◽  
Geneviève Coulombe ◽  
Vanessa Vaillancourt‐Lavigueur ◽  
Christine Jones ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Secretory Cell ◽  
Intestinal Growth ◽  
Homology Region ◽  
Src Homology

Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3 with sequence similarity to the src -homology region 2

FEBS Letters ◽  
1992 ◽  
Vol 314 (3) ◽  
pp. 335-339 ◽  
Author(s):  
Masaaki Adachi ◽  
Masuo Sekiya ◽  
Toshiki Miyachi ◽  
Keiki Matsuno ◽  
Yuji Hinoda ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Protein Tyrosine Phosphatase ◽  
Sequence Similarity ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine ◽  
Homology Region ◽  
Src Homology ◽  
Novel Protein

scholarly journals Deficiency of the Src Homology Region 2 Domain-Containing Phosphatase 1 (SHP-1) Causes Enrichment of CD4+CD25+ Regulatory T Cells

2005 ◽  
Vol 174 (11) ◽  
pp. 6627-6638 ◽  
Author(s):  
Jennifer D. Carter ◽  
Gina M. Calabrese ◽  
Makoto Naganuma ◽  
Ulrike Lorenz
Keyword(s):  
T Cells ◽  
Regulatory T Cells ◽  
Homology Region ◽  
Src Homology

scholarly journals Widespread transcript shortening through alternative polyadenylation in secretory cell differentiation

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Larry C. Cheng ◽  
Dinghai Zheng ◽  
Erdene Baljinnyam ◽  
Fangzheng Sun ◽  
Koichi Ogami ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Secretory Cell ◽  
Alternative Polyadenylation

scholarly journals The common src homology region 2 domain of cytoplasmic signaling proteins is a positive effector of v-fps tyrosine kinase function.

1989 ◽  
Vol 9 (10) ◽  
pp. 4131-4140 ◽  
Author(s):  
C A Koch ◽  
M Moran ◽  
I Sadowski ◽  
T Pawson
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Kinases ◽  
Kinase Activity ◽  
Specific Activity ◽  
Intramolecular Interaction ◽  
Kinase Domain ◽  
Sh2 Domain ◽  
Homology Region ◽  
Src Homology ◽  
Type V

A conserved noncatalytic domain SH2 (for src homology region 2) is located immediately N terminal to the kinase domains of all cytoplasmic protein-tyrosine kinases. We found that the wild-type v-fps SH2 domain stimulated the enzymatic activity of the adjacent kinase domain 10-fold and functioned as a powerful positive effector of catalytic and transforming activities within the v-fps oncoprotein (P130gag-fps). Partial proteolysis of P130gag-fps and supporting genetic data indicated that the v-fps SH2 domain exerts its effect on catalytic activity through an intramolecular interaction with the kinase domain. Amino acid alterations in the SH2 domain that impaired kinase function interfered with association of the SH2 domain with the kinase domain. Deletion of a conserved octapeptide motif converted the v-fps SH2 domain from an activator to an inhibitor of tyrosine kinase activity. This latent inhibitory activity of v-fps SH2 has functional implications for phospholipase C-gamma and p21ras GTPase-activating protein, both of which have two distinct SH2 domains suggestive of complex regulation. In addition to regulating the specific activity of the kinase domain, the SH2 domain of P130gag-fps was also found to be required for the tyrosine phosphorylation of specific cellular proteins, notably polypeptides of 124 and 62 kilodaltons. The SH2 domain therefore appears to play a dual role in regulation of kinase activity and recognition of cellular substrates.

scholarly journals Src homology region 2 domains direct protein-protein interactions in signal transduction.

1990 ◽  
Vol 87 (21) ◽  
pp. 8622-8626 ◽  
Author(s):  
M. F. Moran ◽  
C. A. Koch ◽  
D. Anderson ◽  
C. Ellis ◽  
L. England ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Homology Region ◽  
Src Homology

scholarly journals BCR first exon sequences specifically activate the BCR/ABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias.

1991 ◽  
Vol 11 (4) ◽  
pp. 1785-1792 ◽  
Author(s):  
A J Muller ◽  
J C Young ◽  
A M Pendergast ◽  
M Pondel ◽  
N R Landau ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Cell Transformation ◽  
Philadelphia Chromosome ◽  
Sh3 Domain ◽  
Kinase Domain ◽  
Chromosome Translocation ◽  
Regulatory Domains ◽  
Homology Region ◽  
Abl Tyrosine Kinase ◽  
Src Homology

The c-abl proto-oncogene encodes a cytoplasmic tyrosine kinase which is homologous to the src gene product in its kinase domain and in the upstream kinase regulatory domains SH2 (src homology region 2) and SH3 (src homology region 3). The murine v-abl oncogene product has lost the SH3 domain as a consequence of N-terminal fusion of gag sequences. Deletion of the SH3 domain is sufficient to render the murine c-abl proto-oncogene product transforming when myristylated N-terminal membrane localization sequences are also present. In contrast, the human BCR/ABL oncogene of the Philadelphia chromosome translocation has an intact SH3 domain and its product is not myristylated at the N terminus. To analyze the contribution of BCR-encoded sequences to BCR/ABL-mediated transformation, the effects of a series of deletions and substitutions were assessed in fibroblast and hematopoietic-cell transformation assays. BCR first-exon sequences specifically potentiate transformation and tyrosine kinase activation when they are fused to the second exon of otherwise intact c-ABL. This suggests that BCR-encoded sequences specifically interfere with negative regulation of the ABL-encoded tyrosine kinase, which would represent a novel mechanism for the activation of nonreceptor tyrosine kinase-encoding proto-oncogenes.

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