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Anillin-related Mid1 as an adaptive and multimodal contractile ring anchoring protein: A simulation study
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Abstract
Cytokinesis of animal and fungi cells depends crucially on the anillin scaffold proteins. Fission yeast anillin-related Mid1 anchors cytokinetic ring precursor nodes to the membrane. However, it is unclear if both of its Pleckstrin Homology (PH) and C2 C-terminal domains bind to the membrane as monomers or dimers, and if one domain plays a dominant role. We studied Mid1 membrane binding with all-atom molecular dynamics near a membrane with yeast-like lipid composition. In simulations with the full C terminal region started away from the membrane, Mid1 binds through the disordered L3 loop of C2 in a vertical orientation, with the PH away from the membrane. However, a configuration with both C2 and PH initially bound to the membrane remains associated with the membrane. Simulations of C2-PH dimers show extensive asymmetric membrane contacts. These multiple modes of binding may reflect Mid1's multiple interactions with membranes, node proteins, and ability to sustain mechanical forces.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Self- and actin-templated assembly of Mammalian septins
Kinoshita, M., Field, C. M., Coughlin, M. L., Straight, A. F., & Mitchison, T. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00366-0 · Cited by 526
Muller, M. P., Jiang, T., Sun, C., Lihan, M., Pant, S., Mahinthichaichan, P., Trifan, A., & Tajkhorshid, E. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00608 · Cited by 282
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Metadata
- Authors
- Hall, A. R., Choi, Y. K., Im, W., & Vavylonis, D.
- Affiliations
- Lehigh University (US)
- Corresponding author
- Vavylonis, Dimitrios
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2024-02
- Volume
- 32
- Issue
- 2
- Pages
- 242-252.e2
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC10872332
- OpenAlex
- W4389781434
- Cited by
- 3
- References
- 3
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 366 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Structure (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- PubMed Central (submittedVersion)
- Funders
- National Institutes of Health (R35GM136372)
- Office of Science (2019035, DE-AC02-06CH11357)
- National Science Foundation (MCB-2111728, MCB180021)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- MID1, anillin, contractile ring, cytokinesis, Schizosaccharomyces pombe, pleckstrin homology domain, C2 domain, membrane binding, protein-membrane interactions, mechanical forces
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