PHOSPHORYLATION OF THE NA,K-ATPASE BY CA,PHOSPHOLIPID-DEPENDENT AND CAMP-DEPENDENT PROTEIN-KINASES - MAPPING OF THE REGION PHOSPHORYLATED BY CA,PHOSPHOLIPID-DEPENDENT PROTEIN-KINASE

被引:31
作者
CHIBALIN, AV [1 ]
LOPINA, OD [1 ]
PETUKHOV, SP [1 ]
VASILETS, LA [1 ]
机构
[1] RUSSIAN ACAD SCI,INST CHEM PHYS CHERNOGOLOVKA,MOSCOW,RUSSIA
关键词
NA; K-ATPASE; PROTEIN KINASE-C; PROTEIN KINASE-A; PROTEIN PHOSPHORYLATION; PROTEOLYSIS;
D O I
10.1007/BF00768069
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Ca,phospholipid-dependent (PKC) and cAMP-dependent (PKA) protein kinases phosphorylate the alpha-subunit of the Na,K-ATPase from duck salt gland with the incorporation of 0.3 and 0.5 mol P-32/mol of alpha-subunit, respectively. PKA (in contrast to PKC) phosphorylates the alpha-subunit only in the presence of detergents' Limited tryptic digestion of the Na,K-ATPase phosphorylated by PKC demonstrates that P-32 is incorporated into the N-terminal 41-kDa fragment of the alpha-subunit. Selective chymotrypsin cleavage of phosphorylated enzyme yields a 35-kDa radioactive fragment derived from the central region of the alpha-subunit molecule. These findings suggest that PKC phosphorylates the alpha-subunit of the Na,K-ATPase within the region restricted by C3 and T1 cleavage sites.
引用
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页码:61 / 66
页数:6
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