Molecular Genetics of Kinesin Light Chains: Generation of Isoforms by Alternative Splicing

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 88; no. 22; pp. 10114 - 10118
• Main Authors: Cyr, Janet L., Pfister, K. Kevin, Bloom, George S., Slaughter, Clive A., Brady, Scott T.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 15.11.1991; National Acad Sciences
• Subjects: Amino Acid Sequence; Amino acids; Animals; Base Sequence; Biological and medical sciences; Blotting, Southern; brain; Brain - enzymology; Cell motility; Cloning, Molecular; Complementary DNA; DNA - genetics; DNA - isolation & purification; DNA Probes; Fundamental and applied biological sciences. Psychology; Gene Library; Genes; Isoenzymes - genetics; Kinesin - genetics; Macromolecular Substances; Messenger RNA; Molecular and cellular biology; Molecular chains; Molecular genetics; Molecular Sequence Data; motor protein complex; Open reading frames; Organelles; Protein Conformation; Protein isoforms; Rats; Repetitive Sequences, Nucleic Acid; Restriction Mapping; RNA Splicing; Transcription. Transcription factor. Splicing. Rna processing; Ungulates; Alternative splicing; Molecular form; Molecular processing; Rat; Nucleotide sequence; Rodentia; light-Peptide chain; Vertebrata; Mammalia; Messenger RNA; Complementary DNA; Microtubule associated protein; Aminoacid sequence; Brain (vertebrata)
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.88.22.10114

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.