Journal
JOURNAL OF CELL BIOLOGY
Volume 168, Issue 4, Pages 587-598Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200410114
Keywords
-
Categories
Funding
- NIGMS NIH HHS [R01 GM038499] Funding Source: Medline
- PHS HHS [NIH38499] Funding Source: Medline
- Wellcome Trust [051091] Funding Source: Medline
Ask authors/readers for more resources
EB1 is a member of a conserved protein family that localizes to growing microtubule plus ends. EB1 proteins also recruit cell polarity and signaling molecules to microtubule tips. However, the mechanism by which EB1 recognizes cargo is unknown. Here, we have defined a repeat sequence in adenomatous polyposis coli (APC) that binds to EB1's COOH-terminal domain and identified a similar sequence in members of the microtubule actin cross-linking factor (MACF) family of spectraplakins. We show that MACFs directly bind EB1 and exhibit EB1-dependent plus end tracking in vivo. To understand how EB1 recognizes APC and MACFs, we solved the crystal structure of the EB1 COOH-terminal domain. The structure reveals a novel homodimeric fold comprised of a coiled coil and four-helix bundle motif. Mutational analysis reveals that the cargo binding site for MACFs maps to a cluster of conserved residues at the junction between the coiled coil and four-helix bundle. These results provide a structural understanding of how EB1 binds two regulators of microtubule-based cell polarity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available