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Article

Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition.

Proceedings of the National Academy of Sciences of the United States of America - 19 Jun 2007

Mishima Masaki, Maesaki Ryoko, Kasa Miyuki, Watanabe Takashi, Fukata Masaki, Kaibuchi Kozo, Hakoshima Toshio

Abstract excerpt

Cytoplasmic linker protein 170 (CLIP-170) is a prototype of the plus end-tracking proteins that regulate microtubule dynamics, but it is obscure how CLIP-170 recognizes the microtubule plus end and contributes to polymerization rescue. Crystallographic, NMR, and mutation studies of two tandem cytoskeleton-associated protein glycine-rich (CAP-Gly) domains of CLIP-170, CAP-Gly-1 and CAP-Gly-2, revealed positively...

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Identifiers

PMID: 17563362
DOI: 10.1073/pnas.0703876104
PMCID: PMC1965516

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition.PMID 17563362Read ↗

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