Proline-rich domain in dynamin-2 has a low microtubule-binding activity: how is this activity controlled during mitosis in HeLa cells?
The large GTPase dynamin is strongly accumulated in the constricted area including midzonal microtubules of dividing cells. The proline-rich domain (PRD) of dynamin has been considered as a microtubule-binding domain. However, it remains unclear how PRD controls dynamin-microtubule interaction in mitotic cells. Here, we found that the microtubule-binding activity of PRD is low in dynamin-2. One of the mitosis-specific kinase activities to PRD in HeLa cells was identified as cyclin B-Cdc2 kinase. The kinase phosphorylated PRD at Ser(764) and/or Thr(766) and reduced the microtubule-binding activity of PRD. These results suggest that phosphorylation of PRD by cyclin B-Cdc2 kinase plays an important role to control dynamin-2-microtubule interaction in mitotic HeLa cells.
Morita
Makiko
M
Department of Biological Science, Graduate School of Science, Hiroshima University, Higashi-Hiroshima 739-8526, Japan.
Hamao
Kozue
K
Izumi
Shunsuke
S
Okumura
Eiichi
E
Tanaka
Keita
K
Kishimoto
Takeo
T
Hosoya
Hiroshi
H
D016203:CDC2 Protein Kinase / Q000378:metabolism; D034285:Dynamin II / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008870:Microtubules / Q000378:metabolism*; D008938:Mitosis / Q000502:physiology; D010766:Phosphorylation; D055232:Proline-Rich Protein Domains / Q000502:physiology*
D016203:CDC2 Protein Kinase; D034285:Dynamin II