Direct and indirect effects of tubulin post-translational modifications on microtubule stability: Insights and regulations.

Julia Bär, Yannes Popp, Michael Bucher, Marina Mikhaylova

Journal: Biochimica et biophysica acta. Molecular cell research 2022;1869(6):119241

PMID: 35181405

Free Full Text on Elsevier Science View on PubMed

Abstract

Microtubules (MTs) mediate various cellular functions such as structural support, chromosome segregation, and intracellular transport. To achieve this, the pivotal properties of MTs have to be changeable and tightly controlled. This is enabled by a high variety of tubulin posttranslational modifications, which influence MT properties directly, via altering the MT lattice structurally, or indirectly by changing MT interaction partners. Here, the distinction between these direct and indirect effects of MT PTMs are exemplified by acetylation of the luminal α-tubulin K40 resulting in decreased rigidity of MTs, and by MT detyrosination which decreases interaction with depolymerizing proteins, thus causing more stable MTs. We discuss how these PTMs are reversed and regulated, e.g. on the level of enzyme transcription, localization, and activity via various signalling pathways including the conventional calcium-dependent proteases calpains and how advances in microscopy techniques and development of live-sensors facilitate the understanding of MT PTM interaction and effects.

Address: RG Optobiology, Institute of Biology, Humboldt Universität zu Berlin, Invalidenstr. 42, 10115 Berlin, Germany; Guest Group "Neuronal Protein Transport", Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Falkenried 94, 20251 Hamburg, Germany. Electronic address: [email protected].; RG Optobiology, Institute of Biology, Humboldt Universität zu Berlin, Invalidenstr. 42, 10115 Berlin, Germany; Guest Group "Neuronal Protein Transport", Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Falkenried 94, 20251 Hamburg, Germany. Electronic address: [email protected].; RG Optobiology, Institute of Biology, Humboldt Universität zu Berlin, Invalidenstr. 42, 10115 Berlin, Germany; Guest Group "Neuronal Protein Transport", Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Falkenried 94, 20251 Hamburg, Germany. Electronic address: [email protected].; RG Optobiology, Institute of Biology, Humboldt Universität zu Berlin, Invalidenstr. 42, 10115 Berlin, Germany; Guest Group "Neuronal Protein Transport", Center for Molecular Neurobiology, ZMNH, University Medical Center Hamburg-Eppendorf, Falkenried 94, 20251 Hamburg, Germany. Electronic address: [email protected].

DOI: 10.1016/j.bbamcr.2022.119241

Link outs

Free resources

Full Text Sources:

https://linkinghub.elsevier.com/retrieve/pii/S0167...

Miscellaneous:

https://assays.cancer.gov/CPTAC-1532

MeSH Terms: Acetylation, Microtubules, Protein Processing, Post-Translational, Tubulin