CDK1 phosphorylates condensin I

Stable Identifier
R-HSA-2514854
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

CDK1 (CDC2) in complex with CCNB (cyclin B) phosphorylates condensin I subunits NCAPD2, NCAPG and NCAPH in mitosis (Kimura et al. 2001, Takemoto et al. 2006), but other mitotic kinases may also be involved. CDK1 phosphorylation sites in NCAPH have not been established. NCAPD2 threonine residues T1339, T1384 and T1389 are inferred to be phosphorylated by CDK1 based on homologues sites in Xenopus laevis Ncapd2 (Kimura et al. 1998). NCAPG threonine residues T308 and T332 are phosphorylated by CDK1 in vitro and functionally important. The functional importance of threonine T931, also phosphorylated by CDK1 in vitro, has not been demonstrated (Murphy et al. 2008). Phosphorylation by CDK1 is required for mitotic activation of condensin I and promotes chromosomal binding, introduction of positive supercoils into DNA, and chromatin condensation (Kimura et al. 1998, Kimura et al. 2001, Takemoto et al. 2006).

Literature References
PubMed ID Title Journal Year
18977199 Phosphorylation of CAP-G is required for its chromosomal DNA localization during mitosis

Murphy, LA, Sarge, KD

Biochem. Biophys. Res. Commun. 2008
11136719 Chromosome condensation by a human condensin complex in Xenopus egg extracts

Kimura, K, Cuvier, O, Hirano, T

J. Biol. Chem. 2001
9774278 Phosphorylation and activation of 13S condensin by Cdc2 in vitro

Kimura, K, Hirano, M, Kobayashi, R, Hirano, T

Science 1998
17066080 Negative regulation of condensin I by CK2-mediated phosphorylation

Takemoto, A, Kimura, K, Yanagisawa, J, Yokoyama, S, Hanaoka, F

EMBO J. 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
cyclin-dependent protein serine/threonine kinase activity of CCNB1,CCNB2:p-T161-CDK1 [cytosol]
Physical Entity
Activity
Inferred From
Authored
Reviewed
Created