Kinesin light chains: identification and characterization of a family of proteins from the optic lobe of the squid Loligo pealii

DNA Cell Biol. 1993 Dec;12(10):901-9. doi: 10.1089/dna.1993.12.901.

Abstract

Multiple transcripts coding for kinesin light chain isoforms are present in the tissues of the squid Loligo pealii. Isoform diversity arises through alternative RNA splicing in the amino and carboxyl termini of the putative proteins. Comparison to rat and Drosophila proteins demonstrates a remarkable conservation of structural domains and regulatory motifs. We have identified a PEST domain that may be the site of degradative uncoupling of kinesin functions. Selective transcript distribution occurs in disparate tissues, suggesting an adaptation toward specialized functions. Expression is highest in the nervous system and some evidence for neural-specific transcripts is provided. In neurons, this may relate to the differential targeting of specific membrane-bound organelles such as synaptic vesicles.

MeSH terms

  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary
  • Decapodiformes / chemistry*
  • Decapodiformes / metabolism
  • Drosophila
  • Kinesins / analysis*
  • Kinesins / genetics
  • Kinesins / metabolism
  • Microtubule-Associated Proteins / analysis*
  • Microtubule-Associated Proteins / genetics
  • Microtubule-Associated Proteins / metabolism
  • Molecular Sequence Data
  • Optic Lobe, Nonmammalian / chemistry*
  • Optic Lobe, Nonmammalian / metabolism
  • Organelles / metabolism
  • RNA, Messenger / metabolism
  • Rats
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Microtubule-Associated Proteins
  • RNA, Messenger
  • Kinesins

Associated data

  • GENBANK/L24439
  • GENBANK/L24440
  • GENBANK/L24441