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Identification of a conserved residue responsible for the autoinhibition of cGMP‐dependent protein kinase Iα and β
Author(s) -
Yuasa Keizo,
Michibata Hideo,
Omori Kenji,
Yanaka Noriyuki
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01786-x
Subject(s) - autophosphorylation , protein kinase a , residue (chemistry) , microbiology and biotechnology , protein kinase domain , cgmp dependent protein kinase , kinase , chemistry , mutant , biochemistry , mutagenesis , biology , mitogen activated protein kinase kinase , gene
We isolated a constitutively active form of cGMP‐dependent protein kinase Iα (cGK Iα) by PCR‐driven random mutagenesis. The replacement of Ile‐63 by Thr in the autoinhibitory domain results in the enhancement of autophosphorylation and the basal kinase activity in the absence of cGMP. The hydrophobicity at position 63 is essential for the inactive state of cGK Iα, and Ile‐78 of cGK Iβ is also required for the autoinhibitory property. Furthermore, cGK Iα (Ile‐63‐Thr) is constitutively active in vivo. These findings suggest that a conserved residue in the autoinhibitory domain was involved in the autoinhibition of both cGK Is.