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J. Biol. Chem., Vol. 278, Issue 50, 49721-49731, December 12, 2003

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Characterization of Functional Domains of Human EB1 Family Proteins^*

Wen Bu and Li-Kuo Su

From the Department of Molecular and Cellular Oncology, The University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030

EB1 family proteins are evolutionarily conserved proteins that bind microtubule plus-ends and centrosomes and regulate the dynamics and organization of microtubules. Human EB1 family proteins, which include EB1, EBF3, and RP1, also associate with the tumor suppressor protein adenomatous polyposis coli (APC) and p150^glued, a component of the dynactin complex. The structural basis for interaction between human EB1 family proteins and their associated proteins has not been defined in detail. EB1 family proteins have a calponin homology (CH) domain at their N terminus and an EB1-like C-terminal motif at their C terminus; the functional importance of these domains has not been determined. To better understand functions of human EB1 family proteins and to reveal functional similarities and differences among these proteins, we performed detailed characterizations of interactions between human EB1 family proteins and their associated proteins. We show that amino acids 1–133 of EB1 and EBF3 and the corresponding region of RP1, which contain a CH domain, are necessary and sufficient for binding microtubules, thus demonstrating for the first time that a CH domain contributes to binding microtubules. EB1 family proteins use overlapping but different regions that contain the EB1-like C-terminal motif to associate with APC and p150^glued. Neither APC nor p150^glued binding domain is necessary for EB1 or EBF3 to induce microtubule bundling, which requires amino acids 1–181 and 1–185 of EB1 and EBF3, respectively. We also determined that the EB1 family protein-binding regions are amino acids 2781–2820 and 18–111 of APC and p150^glued, respectively.

Received for publication, June 12, 2003 , and in revised form, September 23, 2003.

^* This work was supported in part by the Gillson Longenbaugh Foundation and NCI, National Institutes of Health, Grant CA 70371 and Cancer Center Core Grant CA 6672. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Dept. of Molecular Genetics, The University of Texas M.D. Anderson Cancer Center, 1515 Holcombe Blvd., Houston, TX 77030.

To whom correspondence should be addressed: Cell Press, 1100 Massachusetts Ave., Cambridge, MA 02138. Tel.: 617-397-2829; Fax: 617-397-2810; E-mail: lsu{at}cell.com.

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