Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes

Glutamylation, introduced by tubulin tyrosine ligase-like (TTLL) enzymes, is the most abundant modification of brain tubulin. Essential effector proteins read the tubulin glutamylation pattern, and its misregulation causes neurodegeneration. TTLL glutamylases post-translationally add glutamates to i...

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Veröffentlicht in:	Nature structural & molecular biology 2020-09, Vol.27 (9), p.802-813
Hauptverfasser:	Mahalingan, Kishore K., Keith Keenan, E., Strickland, Madeleine, Li, Yan, Liu, Yanjie, Ball, Haydn L., Tanner, Martin E., Tjandra, Nico, Roll-Mecak, Antonina
Format:	Artikel
Sprache:	eng
Schlagworte:	631/337 631/45 631/535 631/57 631/80 82 Animals Biochemistry Biological Microscopy Biomedical and Life Sciences Cellular structure Chemical properties Composition Crystallography, X-Ray Elongated structure Elongation Enzymes Glutamate Glutamates Health aspects Life Sciences Membrane Biology Mice Microtubules Models, Molecular Neurodegeneration Peptide Synthases - chemistry Peptide Synthases - metabolism Phylogenetics Phylogeny Polyglutamic Acid - chemistry Polyglutamic Acid - metabolism Post-translation Post-translational modification Protein Conformation Protein Processing, Post-Translational Protein research Protein Structure Proteins Regioselectivity Residues Structure Tubulin Tubulin - chemistry Tubulin - metabolism Tubulins Tyrosine
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