Dynein light chain 1 phosphorylation controls macropinocytosis

Zhibo Yang, Ratna K Vadlamudi, Rakesh Kumar

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Recent studies have identified dynein light chain-1 (DLC1), a component of the dynein motor, as a p21-activated kinase 1 (Pak1)-interacting substrate with binding sites mapped to amino acids 61-89 of DLC1 and phosphorylation site at serine 88. Here we investigated the role of DLC1 phosphorylation by Pak1 upon the process of macropinocytosis. We found that Pak1 associates with dynein motor and that Pak1-DLC1 interaction starts at the initiation of pinosome formation and persists in early and late endosomes. Pak1 phosphorylation of DLC1 on Ser-88 controls vesicle formation and trafficking functions, as Ser-88 substitution for alanine prevents macropinocytosis. A peptide spanning the C-terminal 19-amino acid region of DLC1 efficiently blocked Ser-88 phosphorylation and macropinocytosis. These results suggest that the regulation of DLC1 by Pak1 is a novel mechanism by which a signaling kinase might influence macropinocytosis.

Original languageEnglish (US)
Pages (from-to)654-659
Number of pages6
JournalJournal of Biological Chemistry
Volume280
Issue number1
DOIs
StatePublished - Jan 7 2005
Externally publishedYes

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Dyneins
Phosphorylation
p21-Activated Kinases
Amino Acids
Endosomes
Alanine
Serine
Substitution reactions
Phosphotransferases
Binding Sites
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dynein light chain 1 phosphorylation controls macropinocytosis. / Yang, Zhibo; Vadlamudi, Ratna K; Kumar, Rakesh.

In: Journal of Biological Chemistry, Vol. 280, No. 1, 07.01.2005, p. 654-659.

Research output: Contribution to journalArticle

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