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NAP1L1 is a novel microtubule-associated protein
Nannan Peng1, Yang Zhang1, Xinyue Zhang1
1School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China.
Cytoskeleton (Hoboken, N.J.)
|April 26, 2023
Summary
Nucleosome assembly protein 1 like 1 (NAP1L1) is identified as a novel microtubule-associated protein (MAP). NAP1L1 binds to microtubules and bundles them, influencing cell adhesion and migration.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Biochemistry
Background:
- Microtubule-associated proteins (MAPs) are crucial for microtubule dynamics in various cellular processes.
- Identifying novel MAPs is essential for understanding microtubule regulation.
Purpose of the Study:
- To identify and characterize novel microtubule-associated proteins (MAPs).
- To investigate the role of nucleosome assembly protein 1 like 1 (NAP1L1) as a MAP.
Main Methods:
- Data mining of the Human Protein Atlas and PubMed databases.
- Exogenous expression of candidate proteins with GFP/HA tags and immunofluorescent microscopy.
- Biochemical mapping using bacterially expressed recombinant NAP1L1 fragments and purified microtubules.
- Analysis of RNA-seq data from NAP1L1-depleted cells.
Main Results:
- Nucleosome assembly protein 1 like 1 (NAP1L1) was identified as a novel MAP.
- NAP1L1 localizes with microtubules in the cytosol during interphase.
- The N-terminal (1-72aa) and central (164-269aa) regions of NAP1L1 bind to microtubules.
- NAP1L1 dimerizes via its long helix region (73-163aa) and induces microtubule bundling.
- NAP1L1 depletion affects cell adhesion and migration.
Conclusions:
- NAP1L1 functions as a MAP, capable of bundling microtubules.
- NAP1L1 plays a role in cell adhesion and migration, consistent with its MAP function.
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