Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene

McCart, A. E., Mahony, D. and Rothnagel, J. A. (2003) Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene. Traffic, 4 8: 576-580.


Author McCart, A. E.
Mahony, D.
Rothnagel, J. A.
Title Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene
Journal name Traffic   Check publisher's open access policy
ISSN 1398-9219
Publication date 2003
Sub-type Editorial
DOI 10.1034/j.1600-0854.2003.00113.x
Volume 4
Issue 8
Start page 576
End page 580
Total pages 5
Place of publication Copenhagen
Publisher Blackwell Munksgaard
Collection year 2003
Language eng
Subject C1
270202 Genome Structure
780105 Biological sciences
Abstract Conventional kinesin is a microtubule-based molecular motor involved in the transport of membranous and non-membranous cargoes. The kinesin holoenzyme exists as a heterotetramer, consisting of two heavy chain and two light chain subunits. It is thought that one function of the light chains is to interact with the cargo. Alternative splicing of kinesin light chain pre-mRNA has been observed in lower organisms, although evidence for alternative splicing of the human gene has not been reported. We have identified 19 variants of the human KNS2 gene (KLC1) that are generated by alternative splicing of downstream exons, but calculate that KNS2 has the potential to produce 285919 spliceforms. Corresponding spliceforms of the mouse KLC1 gene were also identified. The alternative exons are all located 3' of exon 12 and the novel spliceforms produce both alternative carboxy termini and alternative 3' untranslated regions. The observation of multiple light chain isoforms is consistent with their proposed role in specific cargo attachment.
Keyword Cell Biology
Alternative Isoforms
Alternative Splicing
Kinesin
Kinesin Light Chain
Multiple Transcripts
Kinesin Light-chain
Fast Axonal-transport
Heavy-chain
Cultured-cells
Isoforms
Identification
Microtubules
Proteins
Motility
Binding
Q-Index Code C1

 
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