Regulation of flagellar assembly by glycogen synthase kinase 3 in Chlamydomonas reinhardtii

Nedra Wilson, Paul A. Lefebvre

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

Chlamydomonas reinhardtii controls flageller 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.

Original languageEnglish
Pages (from-to)1307-1319
Number of pages13
JournalEukaryotic Cell
Volume3
Issue number5
DOIs
StatePublished - 1 Oct 2004

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Glycogen Synthase Kinase 3
Chlamydomonas reinhardtii
Flagella
Lithium
Regeneration
Axoneme
Chlamydomonas
Kinesin
Tyrosine
Signal Transduction
Phosphotransferases
Phosphorylation

Cite this

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Regulation of flagellar assembly by glycogen synthase kinase 3 in Chlamydomonas reinhardtii. / Wilson, Nedra; Lefebvre, Paul A.

In: Eukaryotic Cell, Vol. 3, No. 5, 01.10.2004, p. 1307-1319.

Research output: Contribution to journalArticle

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