cdc2 kinase phosphorylation of desmin at three serine/threonine residues in the amino-terminal head domain.
Phosphorylation of desmin filament by cdc2 kinase induced a transition toward the depolymerized state of the filament. Sequence analysis of purified phosphopeptides derived from cdc2 kinase-phosphorylated desmin revealed that Ser-6, Ser-22 and Thr-64 in the N-terminal head domain were the sites phosphorylated.
Kusubata
M
M
Department of Neurophysiology, Tokyo Metropolitan Institute of Gerontology, Japan.
Matsuoka
Y
Y
Tsujimura
K
K
Ito
H
H
Ando
S
S
Kamijo
M
M
Yasuda
H
H
Ohba
Y
Y
Okumura
E
E
Kishimoto
T
T
D000595:Amino Acid Sequence; D000818:Animals; D016203:CDC2 Protein Kinase / Q000378:metabolism*; D002645:Chickens; D003893:Desmin / Q000737:chemistry / Q000378:metabolism*; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D010769:Phosphothreonine / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism
D003893:Desmin; D010750:Phosphoproteins; D010769:Phosphothreonine; D010768:Phosphoserine; D011494:Protein Kinases; D011493:Protein Kinase C; D016203:CDC2 Protein Kinase