Molecular genetics of kinesin light chains: Generation of isoforms by alternative splicing

Janet L. Cyr, K. Kevin Pfister, George S. Bloom, Clive A. Slaughter, Scott T. Brady

Research output: Contribution to journalArticlepeer-review

117 Scopus citations


Movement of membrane-bounded organelles to intracellular destinations requires properly oriented microtubules and force-generating enzymes, such as the microtubule-stimulated ATPase kinesin. Kinesin is a heterotetramer with two heavy chain (≈124-kDa) and two light chain (≈64-kDa) subunits. Kinesin heavy chains contain both ATP- and microtubule-binding domains and are capable of force generation in vitro. Functions of the light chains are undetermined, although evidence suggests they interact with membrane surfaces. We have used molecular genetic approaches to dissect the kinesin light chain structure. Three distinct kinesin light chain cDNAs were cloned and sequenced from rat brain, and they were found to result from alternative splicing of a single gene. Polypeptides encoded by these cDNAs are identical except for their carboxyl ends. Synthesis of multiple light chains, differing from one another in primary structure, could provide a means of generating multiple, functionally specialized forms of the kinesin holoenzyme.

Original languageEnglish (US)
Pages (from-to)10114-10118
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number22
StatePublished - 1991
Externally publishedYes


  • Fast axonal transport
  • Molecular motors
  • Organelle motility

ASJC Scopus subject areas

  • General


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