HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 18, 16159-16168, May 2, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/18/16159    most recent M213126200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bhullar, B. Articles by van der Hoorn, F. A. Search for Related Content PubMed PubMed Citation Articles by Bhullar, B. Articles by van der Hoorn, F. A. Social Bookmarking                      What's this?

Association of Kinesin Light Chain with Outer Dense Fibers in a Microtubule-independent Fashion^*

Bhupinder Bhullar^§¶, Ying Zhang^§, Albert Junco^¶, Richard Oko, and Frans A. van der Hoorn^**

From the  Department of Biochemistry and Molecular Biology, University of Calgary, Calgary, Alberta T2N 4N1, Canada and the  Department of Anatomy and Cell Biology, Queen's University, Kingston, Ontario K7L 3N6, Canada

Conventional kinesin I motor molecules are heterotetramers consisting of two kinesin light chains (KLCs) and two kinesin heavy chains. The interaction between the heavy and light chains is mediated by the KLC heptad repeat (HR), a leucine zipper-like motif. Kinesins bind to microtubules and are involved in various cellular functions, including transport and cell division. We recently isolated a novel KLC gene, klc3. klc3 is the only known KLC expressed in post-meiotic male germ cells. A monoclonal anti-KLC3 antibody was developed that, in immunoelectron microscopy, detects KLC3 protein associated with outer dense fibers (ODFs), unique structural components of sperm tails. No significant binding of KLC3 with microtubules was observed with this monoclonal antibody. In vitro experiments showed that KLC3-ODF binding occurred in the absence of kinesin heavy chains or microtubules and required the KLC3 HR. ODF1, a major ODF protein, was identified as the KLC3 binding partner. The ODF1 leucine zipper and the KLC3 HR mediated the interaction. These results identify and characterize a novel interaction between a KLC and a non-microtubule macromolecular structure and suggest that KLC3 could play a microtubule-independent role during formation of sperm tails.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				C. Fitzgerald, C. Sikora, V. Lawson, K. Dong, M. Cheng, R. Oko, and F. A. van der Hoorn Mammalian Transcription in Support of Hybrid mRNA and Protein Synthesis in Testis and Lung J. Biol. Chem., December 15, 2006; 281(50): 38172 - 38180. [Abstract] [Full Text] [PDF]

				W. Cao, G. L. Gerton, and S. B. Moss Proteomic Profiling of Accessory Structures from the Mouse Sperm Flagellum Mol. Cell. Proteomics, May 1, 2006; 5(5): 801 - 810. [Abstract] [Full Text] [PDF]

				J. G. Gindhart Towards an understanding of kinesin-1 dependent transport pathways through the study of protein-protein interactions Brief Funct Genomic Proteomic, March 1, 2006; 5(1): 74 - 86. [Abstract] [Full Text] [PDF]

				K.-D. Hinsch, V. De Pinto, V. A. Aires, X. Schneider, A. Messina, and E. Hinsch Voltage-dependent Anion-selective Channels VDAC2 and VDAC3 Are Abundant Proteins in Bovine Outer Dense Fibers, a Cytoskeletal Component of the Sperm Flagellum J. Biol. Chem., April 9, 2004; 279(15): 15281 - 15288. [Abstract] [Full Text] [PDF]