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Updated: Sep 27, 2025
08:02
Extracting Modified Microtubules from Mammalian Cells to Study Microtubule-Protein Complexes by Cryo-Electron Microscopy
Published on: March 3, 2023
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The evolution of microtubule associated proteins - a reference proteomic perspective
Amy C Gottschalk1,2, Marco M Hefti3
1College of Liberal Arts and Sciences, University of Iowa, Iowa City, USA.
BMC Genomics
|April 7, 2022
Summary
This study analyzed microtubule associated proteins (MAPs) across eukaryotes, revealing evolutionary relationships and variations in MAP numbers. Findings confirm known MAP phylogenies and offer new insights into their structure and function.
Area of Science:
- Cell Biology
- Evolutionary Biology
- Proteomics
Background:
- Microtubule associated proteins (MAPs) regulate neuronal microtubule stability.
- Previous evolutionary studies of MAPs used limited genomic data.
Purpose of the Study:
- To conduct a comprehensive phylogenetic analysis of MAPs in vertebrates and invertebrates.
- To explore evolutionary relationships and variations in MAPs using large-scale proteomic data.
Main Methods:
- Utilized public reference-quality eukaryotic proteomes from UniProt.
- Identified MAPs via InterProScan, aligned with MUSCLE, and constructed phylogenetic trees using the WAG algorithm.
- Analyzed 889 proteins with tubulin binding domains across eukaryotes.
Main Results:
- Identified 663 MAPs in eukaryotes, including 168 vertebrates and 64 invertebrates.
- Vertebrate MAPs formed three families (MAP2, MAP4, MAPT); invertebrate MAPs clustered separately.
- Observed significant variation in MAP numbers and binding domains, with fish and mollusks showing high counts.
Conclusions:
- Provided a novel evolutionary analysis of MAPs using extensive proteomic datasets.
- Confirmed existing MAP phylogenies and uncovered new information on MAP structure and function.
- Highlighted significant evolutionary diversity in microtubule associated proteins across taxa.
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