PMID- 15470259
OWN - NLM
STAT- MEDLINE
DCOM- 20050311
LR  - 20211203
IS  - 1535-9778 (Print)
IS  - 1535-9786 (Electronic)
IS  - 1535-9786 (Linking)
VI  - 3
IP  - 5
DP  - 2004 Oct
TI  - Regulation of flagellar assembly by glycogen synthase kinase 3 in Chlamydomonas 
      reinhardtii.
PG  - 1307-19
AB  - Chlamydomonas reinhardtii controls flagellar assembly such that flagella are of 
      an equal and predetermined length. Previous studies demonstrated that lithium, an 
      inhibitor of glycogen synthase kinase 3 (GSK3), induced flagellar elongation, 
      suggesting that a lithium-sensitive signal transduction pathway regulated 
      flagellar length (S. Nakamura, H. Takino, and M. K. Kojima, Cell Struct. Funct. 
      12:369-374, 1987). Here, we demonstrate that lithium treatment depletes the pool 
      of flagellar proteins from the cell body and that the heterotrimeric kinesin 
      Fla10p accumulates in flagella. We identify GSK3 in Chlamydomonas and demonstrate 
      that its kinase activity is inhibited by lithium in vitro. The 
      tyrosine-phosphorylated, active form of GSK3 was enriched in flagella and GSK3 
      associated with the axoneme in a phosphorylation-dependent manner. The level of 
      active GSK3 correlated with flagellar length; early during flagellar 
      regeneration, active GSK3 increased over basal levels. This increase in active 
      GSK3 was rapidly lost within 30 min of regeneration as the level of active GSK3 
      decreased relative to the predeflagellation level. Taken together, these results 
      suggest a possible role for GSK3 in regulating the assembly and length of 
      flagella.
FAU - Wilson, Nedra F
AU  - Wilson NF
AD  - Department of Plant Biology, University of Minnesota, 250 Biological Sciences 
      Center, 1445 Gortner Ave., St. Paul, MN 55108, USA. nwilson@biosci.cbs.umn.edu.
FAU - Lefebvre, Paul A
AU  - Lefebvre PA
LA  - eng
GR  - F32 GM020149/GM/NIGMS NIH HHS/United States
GR  - R01 GM034437/GM/NIGMS NIH HHS/United States
GR  - 5F32-GM20149/GM/NIGMS NIH HHS/United States
GR  - GM34437/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Eukaryot Cell
JT  - Eukaryotic cell
JID - 101130731
RN  - 0 (Algal Proteins)
RN  - 0 (DNA, Protozoan)
RN  - 0 (Enzyme Inhibitors)
RN  - 0 (KHP1 protein, Chlamydomonas)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Protozoan Proteins)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.7.11.26 (Glycogen Synthase Kinase 3)
RN  - G4962QA067 (Lithium Chloride)
SB  - IM
MH  - Algal Proteins
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Chlamydomonas reinhardtii/*enzymology/genetics/*growth & development
MH  - Cloning, Molecular
MH  - DNA, Protozoan/genetics
MH  - Enzyme Inhibitors/pharmacology
MH  - Flagella/drug effects/*enzymology/physiology
MH  - Genes, Protozoan
MH  - Glycogen Synthase Kinase 3/antagonists & inhibitors/genetics/*metabolism
MH  - Lithium Chloride/pharmacology
MH  - Microtubule-Associated Proteins/genetics/metabolism
MH  - Molecular Sequence Data
MH  - Phenotype
MH  - Phosphorylation
MH  - Protozoan Proteins/genetics/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Tyrosine/metabolism
PMC - PMC522593
EDAT- 2004/10/08 09:00
MHDA- 2005/03/12 09:00
PMCR- 2004/10/01
CRDT- 2004/10/08 09:00
PHST- 2004/10/08 09:00 [pubmed]
PHST- 2005/03/12 09:00 [medline]
PHST- 2004/10/08 09:00 [entrez]
PHST- 2004/10/01 00:00 [pmc-release]
AID - 3/5/1307 [pii]
AID - 0029-04 [pii]
AID - 10.1128/EC.3.5.1307-1319.2004 [doi]
PST - ppublish
SO  - Eukaryot Cell. 2004 Oct;3(5):1307-19. doi: 10.1128/EC.3.5.1307-1319.2004.