Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain

1979 ◽  
Vol 158 (1) ◽  
Author(s):  
Bin Xu ◽  
W.Todd Miller
Keyword(s):  
Tyrosine Kinase ◽  
Catalytic Domain ◽  
Active Conformation ◽  
Kinase Catalytic Domain ◽  
Src Homology ◽  
Src Homology Domains ◽  
Homology Domains

scholarly journals Inhibition of VRAC by c-Src tyrosine kinase targeted to caveolae is mediated by the Src homology domains

2001 ◽  
Vol 281 (1) ◽  
pp. C248-C256 ◽  
Author(s):  
Dominique Trouet ◽  
Iris Carton ◽  
Diane Hermans ◽  
Guy Droogmans ◽  
Bernd Nilius ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Inhibitory Effect ◽  
Kinase Domain ◽  
Wild Type ◽  
Patch Clamp Technique ◽  
Src Tyrosine Kinase ◽  
Src Homology ◽  
Cpae Cells ◽  
Src Homology Domains ◽  
Homology Domains

We used the whole cell patch-clamp technique in calf pulmonary endothelial (CPAE) cells to investigate the effect of wild-type and mutant c-Src tyrosine kinase on I Cl,swell, the swelling-induced Cl−current through volume-regulated anion channels (VRAC). Transient transfection of wild-type c-Src in CPAE cells did not significantly affect I Cl,swell. However, transfection of c-Src with a Ser3Cys mutation that introduces a dual acylation signal and targets c-Src to lipid rafts and caveolae strongly repressed hypotonicity-induced I Cl,swell in CPAE cells. Kinase activity was dispensable for the inhibition of I Cl,swell, since kinase-deficient c-Src Ser3Cys either with an inactivating point mutation in the kinase domain or with the entire kinase domain deleted still suppressed VRAC activity. Again, the Ser3Cys mutation was required to obtain maximal inhibition by the kinase-deleted c-Src. In contrast, the inhibitory effect was completely lost when the Src homology domains 2 and 3 were deleted in c-Src. We therefore conclude that c-Src-mediated inhibition of VRAC requires compartmentalization of c-Src to caveolae and that the Src homology domains 2 and/or 3 are necessary and sufficient for inhibition.

scholarly journals Src Homology Domains of Phospholipase C γ1 Inhibit Nerve Growth Factor-Induced Differentiation of PC12 Cells

2002 ◽  
Vol 71 (1) ◽  
pp. 178-185 ◽  
Author(s):  
Sun Sik Bae ◽  
Young Han Lee ◽  
Jong-Soo Chang ◽  
Sehamuddin H. Galadari ◽  
Yong Sik Kim ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Phospholipase C ◽  
Pc12 Cells ◽  
Induced Differentiation ◽  
Nerve Growth ◽  
Src Homology ◽  
Src Homology Domains ◽  
Homology Domains

scholarly journals Cooperation of Src Homology Domains in the Regulated Binding of Phosphatidylinositol 3-Kinase

1995 ◽  
Vol 270 (14) ◽  
pp. 7937-7943 ◽  
Author(s):  
Burkhard Haefner ◽  
Ruth Baxter ◽  
Valerie J. Fincham ◽  
C. Peter Downes ◽  
Margaret C. Frame
Keyword(s):  
Phosphatidylinositol 3 Kinase ◽  
Src Homology ◽  
Src Homology Domains ◽  
Phosphatidylinositol 3 ◽  
Homology Domains

cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases

1990 ◽  
Vol 10 (12) ◽  
pp. 6316-6324
Author(s):  
R A Lindberg ◽  
T Hunter
Keyword(s):  
Protein Kinase ◽  
Tyrosine Kinase ◽  
Tyrosine Kinases ◽  
Protein Tyrosine Kinase ◽  
Catalytic Domain ◽  
Protein Tyrosine Kinases ◽  
Receptor Protein ◽  
Protein Tyrosine ◽  
Kinase Catalytic Domain ◽  
Receptor Protein Tyrosine Kinase

A human epithelial (HeLa) cDNA library was screened with degenerate oligonucleotides designed to hybridize to highly conserved regions of protein-tyrosine kinases. One cDNA from this screen was shown to contain a putative protein-tyrosine kinase catalytic domain and subsequently used to isolate another cDNA from a human keratinocyte library that encompasses the entire coding region of a 976-amino-acid polypeptide. The predicted protein has an external domain of 534 amino acids with a presumptive N-terminal signal peptide, a transmembrane domain, and a cytoplasmic domain of 418 amino acids that includes a canonical protein-tyrosine kinase catalytic domain. Molecular phylogeny indicates that this protein kinase is closely related to eph and elk and that this receptor family is more closely related to the non-receptor protein-tyrosine kinase families than to other receptor protein-tyrosine kinases. Antibodies raised against a TrpE fusion protein immunoprecipitated a 130-kDa protein that became phosphorylated on tyrosine in immune complex kinase assays, indicating that this protein is a bona fide protein-tyrosine kinase. Analysis of RNA from 13 adult rat organs showed that the eck gene is expressed most highly in tissues that contain a high proportion of epithelial cells, e.g., skin, intestine, lung, and ovary. Several cell lines of epithelial origin were found to express the eck protein kinase at the protein and RNA levels. Immunohistochemical analysis of several rat organs also showed staining in epithelial cells. These observations prompted us to name this protein kinase eck, for epithelial cell kinase.

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