Threonine phosphorylation of integrin β3 in calyculin A-treated platelets is selectively sensitive to 5′-iodotubercidin
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Regulation of natural killer cell-mediated cytotoxicity by serine/threonine phosphatases: identification of a calyculin A-sensitive serine/threonine kinase.
We have recently reported that Ser/Thr phosphatases play a key role in regulating natural killer (NK) cell lytic activity and that calyculin A and okadaic acid affect this activity differently [Bajpai and Brahmi (1994) J. Biol. Chem. 269, 18864-18869]. Here, we investigate a mechanism that might account for this differential action of calyculin A and okadaic acid on NK cells. Calyculin A specif...
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The exposure of ligand-binding sites for adhesive proteins on platelet integrin α IIB }β $ (glycoprotein IIB}IIIA) by plateletactivating factor (PAF) is transient, whereas sites exposed by αthrombin remain accessible. The same difference is seen in the phosphorylation of the β $ subunit. Inhibition of protein kinases (1 μM staurosporine) and protein kinase C (10 μM bisindolylmaleimide) closes b...
متن کاملPKD2 and RSK1 Regulate Integrin β4 Phosphorylation at Threonine 1736.
The integrin α6β4, a major component of hemidesmosomes (HDs), stabilizes keratinocyte cell adhesion to the epidermal basement membrane through binding to the cytoskeletal linker protein plectin and association with keratin filaments. Disruption of the α6β4-plectin interaction through phosphorylation of the β4 subunit results in a reduction in adhesive strength of keratinocytes to laminin-332 an...
متن کاملPhosphorylation of threonine 1736 in the C-terminal tail of integrin β4 contributes to hemidesmosome disassembly
During wound healing, hemidesmome disassembly enables keratinocyte migration and proliferation. Hemidesmosome dynamics are altered downstream of epidermal growth factor (EGF) receptor activation, following the phosphorylation of integrin β4 residues S1356 and S1364, which reduces the interaction with plectin; however, this event is insufficient to drive complete hemidesmome disassembly. In the ...
متن کاملNHE3 function and phosphorylation are regulated by a calyculin A-sensitive phosphatase.
Na+/H+ exchanger 3 (NHE3) is phosphorylated and regulated by multiple kinases, including PKA, SGK1, and CK2; however, the role of phosphatases in the dephosphorylation and regulation of NHE3 remains unknown. The purpose of this study was to determine whether serine/threonine phosphatases alter NHE3 activity and phosphorylation and, if so, at which sites. To this end, we first examined the effec...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2007
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2006.08.053