Complex formation of EphB1/Nck/Caskin1 leads to tyrosine phosphorylation and structural changes of the Caskin1 SH3 domain [PDF]
Background Scaffold proteins have an important role in the regulation of signal propagation. These proteins do not possess any enzymatic activity but can contribute to the formation of multiprotein complexes. Although scaffold proteins are present in all
Pesti Szabolcs +6 more
doaj +3 more sources
NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22 [PDF]
Erratum for: NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase ...
Marianne R. Spalinger +19 more
doaj +4 more sources
Tyrosine kinases are crucial signaling components of diverse biological processes and are major therapeutic targets in various malignancies and immune-mediated disorders.
Krisztina Futosi +7 more
doaj +1 more source
Receptor tyrosine kinase (RTK) mediated tyrosine phosphor-proteome from Drosophila S2 (ErbB1) cells reveals novel signaling networks. [PDF]
Protein phosphorylation mediates many critical cellular responses and is essential for many biological functions during development. About one-third of cellular proteins are phosphorylated, representing the phosphor-proteome, and phosphorylation can ...
Srinivasan Krishnamoorthy
doaj +1 more source
Tyrosine Phosphorylation of SGEF Regulates RhoG Activity and Cell Migration. [PDF]
SGEF and Ephexin4 are members of the Ephexin subfamily of RhoGEFs that specifically activate the small GTPase RhoG. It is reported that Ephexin1 and Ephexin5, two well-characterized Ephexin subfamily RhoGEFs, are tyrosine-phosphorylated by Src, and that ...
Yusuke Okuyama +3 more
doaj +1 more source
Extracellular phosphorylation of a receptor tyrosine kinase controls synaptic localization of NMDA receptors and regulates pathological pain. [PDF]
Extracellular phosphorylation of proteins was suggested in the late 1800s when it was demonstrated that casein contains phosphate. More recently, extracellular kinases that phosphorylate extracellular serine, threonine, and tyrosine residues of numerous ...
Kenji Hanamura +11 more
doaj +1 more source
Tyrosine phosphorylation and bacterial virulence [PDF]
Protein phosphorylation on tyrosine has emerged as a key device in the control of numerous cellular functions in bacteria. In this article, we review the structure and function of bacterial tyrosine kinases and phosphatases. Phosphorylation is catalyzed by autophosphorylating adenosine triphosphate-dependent enzymes (bacterial tyrosine (BY) kinases ...
Whitmore, Sarah E, Lamont, Richard J
openaire +2 more sources
Cortactin tyrosine phosphorylation promotes its deacetylation and inhibits cell spreading. [PDF]
BACKGROUND: Cortactin is a classical Src kinase substrate that participates in actin cytoskeletal dynamics by activating the Arp2/3 complex and interacting with other regulatory proteins, including FAK.
Eugenia Meiler +2 more
doaj +1 more source
Characterization of in vivo keratin 19 phosphorylation on tyrosine-391. [PDF]
Keratin polypeptide 19 (K19) is a type I intermediate filament protein that is expressed in stratified and simple-type epithelia. Although K19 is known to be phosphorylated on tyrosine residue(s), conclusive site-specific characterization of these ...
Qin Zhou +7 more
doaj +1 more source
Tyrosine phosphorylation in brassinosteroid signaling [PDF]
Brassinosteroids (BRs) regulate plant growth and development through a complex signal transduction pathway involving BRASSINOSTEROID INSENSITIVE 1 (BRI1), which is the BR receptor, and its co-receptor BRI1-ASSOCIATED KINASE 1 (BAK1). Both proteins are classified as Ser/Thr protein kinases. Recently, we reported that recombinant cytoplasmic domains (CD)
Man-Ho, Oh +2 more
openaire +2 more sources

