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Cryo-EM micrographs of human α1B/βI+βIVb microtubules bound to GMPCPP decorated with TTLL6

ABSTRACT:

SUBMITTER: Antonina Roll-Mecak

PROVIDER: EMPIAR-11798 | biostudies-other |

REPOSITORIES: biostudies-other

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Structural basis for α-tubulin-specific and modification state-dependent glutamylation.

Mahalingan Kishore K KK Grotjahn Danielle A DA Li Yan Y Lander Gabriel C GC Zehr Elena A EA Roll-Mecak Antonina A

Nature chemical biology 20240424 11

Microtubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. How TTLLs specialize for specific substrate recognition and ultimately modification-pattern generation is largely unknown. TTLL6, a glutamylase implicated in ciliopathies, preferentially modifies tubulin α-tails in microtubules. Cryo-electron microscopy, kinetic analysis and single-molecule biochemis ...[more]

PMID: 38658656

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