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Molecular and Cellular Biology, September 2001, p. 6044-6055, Vol. 21, No. 17
Institute of Medical Microbiology,
Immunology, and Hygiene, Technical University of Munich, D-81675
Munich, Germany
Received 28 November 2000/Returned for modification 20 March
2001/Accepted 23 May 2001
The mechanism of cargo coupling to kinesin motor proteins is a
fundamental issue in organelle transport along microtubules. Kinectin
has been postulated to function as a membrane anchor protein that
attaches various organelles to the prototype motor protein kinesin. To
verify the biological relevance of kinectin in vivo, the murine
kinectin gene was disrupted by homologous recombination. Unexpectedly,
kinectin-deficient mice were viable and fertile, and no gross
abnormalities were observed up to 1 year of age. The assembly of the
endoplasmic reticulum was essentially unaffected in kinectin-deficient
cells. Mitochondria appeared to be correctly distributed throughout the
cytoplasm along the microtubules. Furthermore, the stationary
distribution and the bidirectional movement of lysosomes did not depend
on kinectin. Kinectin-deficient phagocytes internalized and cleared
bacteria, indicating that phagosome trafficking and maturation are
functional without kinectin. Thus, these data unequivocally indicate
that kinectin is not essential for trafficking of lysosomes,
phagosomes, and mitochondria in vivo.
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.17.6044-6055.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Intact Lysosome Transport and Phagosome Function
Despite Kinectin Deficiency
and
*
Corresponding author. Mailing address: Institute of
Medical Microbiology, Immunology & Hygiene, Technical University of
Munich, Trogerstrasse 9, D-81675 Munich, Germany. Phone:
49-89-4140-4132. Fax: 49-89-4140-4139. E-mail:
klaus.pfeffer{at}lrz.tum.de.
Present address: Serono Pharmaceutical Research Institute, CH-1228
Geneva, Switzerland.
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