High impact information on Klc1

• Dominant-negative mutants of conventional kinesin light chain blocked outward GLUT4 vesicle movements and translocation of exofacial Myc-tagged GLUT4-green fluorescent protein to the plasma membrane in response to insulin [1].
• We have used molecular genetic approaches to dissect the kinesin light chain structure [2].
• 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 [2].
• KLC3 is able to bind in vitro to mitochondria from spermatids as well as somatic cells employing a conserved kinesin light chain motif, the tetratrico-peptide repeats [3].
• We recently discovered that in rat spermatids, kinesin light chain KLC3 can associate with outer dense fibers, major sperm tail components, and accumulates in the sperm midpiece [3].

Biological context of Klc1

• Here we report that phosphorylation of HAP1 decreases its association with microtubule-dependent transport proteins dynactin p150 and kinesin light chain and reduces its localization in neurite tips [4].

Anatomical context of Klc1

• Our results indicate that the rat spermatid kinesin light chain KLC3 can associate with mitochondria [3].

Other interactions of Klc1

• To prove the reliability of the method, prototypically, the differential expression profiles of three candidate genes (kinesin light chain, ferritin, RYB-A) were verified [5].

References