High impact information on Ktn1

• This is the first study using a single in vitro system that describes the roles played by kinesin, kinectin, cytoplasmic dynein, and dynactin in the microtubule-mediated movement of a purified membrane organelle [1].
• The assembly of the endoplasmic reticulum was essentially unaffected in kinectin-deficient cells [2].
• Intact lysosome transport and phagosome function despite kinectin deficiency [2].
• Furthermore, the stationary distribution and the bidirectional movement of lysosomes did not depend on kinectin [2].
• Kinectin has been postulated to function as a membrane anchor protein that attaches various organelles to the prototype motor protein kinesin [2].

Biological context of Ktn1

• Assignment of the murine kinectin gene (Ktn1) to mouse chromosome 14C2 by fluorescence in situ hybridization [3].
• We also demonstrated in vivo by overexpression and RNA interference assay that kinectin is selectively involved in the transport of specific types of organelles [4].
• The amino acid sequence deduced from kinectin cDNA isolated from mouse spleen cell and testis libraries revealed a long signal peptide or transmembrane sequence, and a 328 amino acid residue globular N-terminal domain adjacent to a much larger 858-999-residue C-terminal coiled-coil rod domain [5].
• The results presented in this article suggest that kinectin is required for spermatogenesis, but is not a likely candidate for use in immunocontraceptive vaccines [6].
• Kinectin was isolated and characterized from a fox testis cDNA library using a monoclonal antibody (FTA-1) raised against testis surface proteins [6].

Anatomical context of Ktn1

• Kinectin-deficient phagocytes internalized and cleared bacteria, indicating that phagosome trafficking and maturation are functional without kinectin [2].
• A 120 kDa kinectin species is specifically associated with mitochondria, and its interaction with kinesin was found to influence mitochondrial dynamics [4].

Analytical, diagnostic and therapeutic context of Ktn1

• Sequence analysis and comparisons between species revealed that kinectin encodes multiple alpha-helical coiled coils predicted to form dimers, and is, therefore, likely to exist as a dimer [6].
• Molecular cloning and characterization of fox testis kinectin [6].

References