2QK0

Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170 and EB1

Summary for 2QK0

• Entry DOI: 10.2210/pdb2qk0/pdb
• Related: 2QJX 2QJZ 2QK1 2QK2
• Descriptor: CAP-Gly domain-containing linker protein 1 (2 entities in total)
• Functional Keywords: clip-170, cap-gly domain, microtubule plus end, +tip, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P30622
• Total number of polymer chains: 1
• Total formula weight: 8243.24

Authors

Slep, K.C.,Vale, R.D. (deposition date: 2007-07-09, release date: 2007-10-02, Last modification date: 2024-11-06)

Primary citation

Slep, K.C.,Vale, R.D.
Structural Basis of Microtubule Plus End Tracking by XMAP215, CLIP-170, and EB1.
Mol.Cell, 27:976-991, 2007

PubMed Abstract: Microtubule plus end binding proteins (+TIPs) localize to the dynamic plus ends of microtubules, where they stimulate microtubule growth and recruit signaling molecules. Three main +TIP classes have been identified (XMAP215, EB1, and CLIP-170), but whether they act upon microtubule plus ends through a similar mechanism has not been resolved. Here, we report crystal structures of the tubulin binding domains of XMAP215 (yeast Stu2p and Drosophila Msps), EB1 (yeast Bim1p and human EB1), and CLIP-170 (human), which reveal diverse tubulin binding interfaces. Functional studies, however, reveal a common property that native or artificial dimerization of tubulin binding domains (including chemically induced heterodimers of EB1 and CLIP-170) induces tubulin nucleation/assembly in vitro and, in most cases, plus end tracking in living cells. We propose that +TIPs, although diverse in structure, share a common property of multimerizing tubulin, thus acting as polymerization chaperones that aid in subunit addition to the microtubule plus end.

PubMed: 17889670
DOI: 10.1016/j.molcel.2007.07.023

Experimental method

X-RAY DIFFRACTION (2 Å)