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J. Biol. Chem., Vol. 277, Issue 2, 1301-1309, January 11, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/2/1301    most recent M106628200v1 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 Eichenmüller, B. Articles by Suprenant, K. A. Search for Related Content PubMed PubMed Citation Articles by Eichenmüller, B. Articles by Suprenant, K. A. Social Bookmarking                      What's this?

The Human EMAP-like Protein-70 (ELP70) Is a Microtubule Destabilizer That Localizes to the Mitotic Apparatus^*

Bernd Eichenmüller, Patrick Everley, Jean Palange, Denise Lepley, and Kathy A. Suprenant

From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045

In this report, we show that the echinoderm microtubule (MT)-associated protein (EMAP) and related EMAP-like proteins (ELPs) share a similar domain organization with a highly conserved hydrophobic ELP (HELP) domain and a large tryptophan-aspartic acid (WD) repeat domain. To determine the function of mammalian ELPs, we generated antibodies against a 70-kDa human ELP and showed that ELP70 coassembled with MTs in HeLa cell extracts and colocalized with MTs in the mitotic apparatus. To determine whether ELP70 bound to MTs directly, human ELP70 was expressed and purified to homogeneity from baculovirus-infected Sf9 cells. Purified ELP70 bound to purified MTs with a stoichiometry of 0.40 ± 0.04 mol of ELP70/mol of tubulin dimer and with an intrinsic dissociation constant of 0.44 ± 0.13 µM. Using a nucleated assembly assay and video-enhanced differential interference contrast microscopy, we demonstrated that ELP70 reduced seeded nucleation, reduced the growth rate, and promoted MT catastrophes in a concentration-dependent manner. As a result, ELP70-containing MTs were significantly shorter than MTs assembled from tubulin alone. These data indicate that ELP70 is a novel MT destabilizer. A lateral destabilization model is presented to describe ELP70's effects on microtubules.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF103939, U97018, and AAG09279.

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