Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor complex. In vitro binding assays indicate an interaction between second cytosolic domain (CD2) of Na/K-ATPase α1 subunit and Src SH2 domain. Since SH2 domain targets Src to specific signaling complexes, we expressed CD2 as a cytosolic protein and studied whether it could act as a Src SH2 ligand in LLC-PK1 cells. Co-immunoprecipitation analy-ses indicated a direct binding of CD2 to Src, consistent with the in vitro binding data. Func-tionally, CD2 expression increased basal Src activity, suggesting a Src SH2 ligand-like property of CD2. Consistently, we found that CD2 expression attenuated several signaling pathways where Src plays an important ...
The role of the nonreceptor tyrosine kinase Src in up-regulating NMDAR activity via phosphorylating ...
Background: Shp1, a tyrosine-phosphatase-1 containing the Src-homology 2 (SH2) domain, is involved i...
Angiotensin (Ang) II is the major bioactive peptide of the renin–angiotensin system (RAS); it contri...
<div><p>Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a rec...
Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor co...
Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor co...
i Na/K-ATPase interacts with Src to form a functional receptor for endogenous cardiotonic steroids s...
Contains fulltext : 108799.pdf (publisher's version ) (Closed access)Digitalis-lik...
We have shown that Na/K-ATPase interacts with Src. Here, we test the role of this interaction in H2O...
Arrestins were originally described as proteins recruited to ligand-activated, phosphorylated G prot...
Contains fulltext : 97222.pdf (publisher's version ) (Open Access)SRC proteins are...
AbstractBackground: The observations that Src−/− mice develop osteopetrosis and Src family tyrosine ...
ShcA is a protein that is recruited to receptor-protein tyrosine kinases, where it is phosphorylated...
The Src-homology 2 (SH2) domain is a protein interaction domain that directs myriad phosphotyrosine ...
Abstract The non-receptor tyrosine kinase Src is a crit-ical regulator of cytoskeletal contraction, ...
The role of the nonreceptor tyrosine kinase Src in up-regulating NMDAR activity via phosphorylating ...
Background: Shp1, a tyrosine-phosphatase-1 containing the Src-homology 2 (SH2) domain, is involved i...
Angiotensin (Ang) II is the major bioactive peptide of the renin–angiotensin system (RAS); it contri...
<div><p>Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a rec...
Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor co...
Our previous studies have suggested that the α1 Na/K-ATPase interacts with Src to form a receptor co...
i Na/K-ATPase interacts with Src to form a functional receptor for endogenous cardiotonic steroids s...
Contains fulltext : 108799.pdf (publisher's version ) (Closed access)Digitalis-lik...
We have shown that Na/K-ATPase interacts with Src. Here, we test the role of this interaction in H2O...
Arrestins were originally described as proteins recruited to ligand-activated, phosphorylated G prot...
Contains fulltext : 97222.pdf (publisher's version ) (Open Access)SRC proteins are...
AbstractBackground: The observations that Src−/− mice develop osteopetrosis and Src family tyrosine ...
ShcA is a protein that is recruited to receptor-protein tyrosine kinases, where it is phosphorylated...
The Src-homology 2 (SH2) domain is a protein interaction domain that directs myriad phosphotyrosine ...
Abstract The non-receptor tyrosine kinase Src is a crit-ical regulator of cytoskeletal contraction, ...
The role of the nonreceptor tyrosine kinase Src in up-regulating NMDAR activity via phosphorylating ...
Background: Shp1, a tyrosine-phosphatase-1 containing the Src-homology 2 (SH2) domain, is involved i...
Angiotensin (Ang) II is the major bioactive peptide of the renin–angiotensin system (RAS); it contri...