4XH3
Mechanistic insights into anchorage of the contractile ring from yeast to humans
Summary for 4XH3
| Entry DOI | 10.2210/pdb4xh3/pdb |
| Related | 4XOH 4XOI |
| Descriptor | Actin-binding protein anillin (2 entities in total) |
| Functional Keywords | c2, cell cycle |
| Biological source | Homo sapiens (Human) |
| Cellular location | Nucleus: Q9NQW6 |
| Total number of polymer chains | 1 |
| Total formula weight | 46765.29 |
| Authors | Sun, L.F.,Guan, R.F.,Chen, Z.C. (deposition date: 2015-01-04, release date: 2015-07-15, Last modification date: 2024-05-29) |
| Primary citation | Sun, L.,Guan, R.,Lee, I.J.,Liu, Y.,Chen, M.,Wang, J.,Wu, J.Q.,Chen, Z. Mechanistic insights into the anchorage of the contractile ring by anillin and mid1 Dev.Cell, 33:413-426, 2015 Cited by PubMed Abstract: Anillins and Mid1 are scaffold proteins that play key roles in anchorage of the contractile ring at the cell equator during cytokinesis in animals and fungi, respectively. Here, we report crystal structures and functional analysis of human anillin and S. pombe Mid1. The combined data show anillin contains a cryptic C2 domain and a Rho-binding domain. Together with the tethering PH domain, three membrane-associating elements synergistically bind to RhoA and phospholipids to anchor anillin at the cleavage furrow. Surprisingly, Mid1 also binds to the membrane through a cryptic C2 domain. Dimerization of Mid1 leads to high affinity and preference for PI(4,5)P2, which stably anchors Mid1 at the division plane, bypassing the requirement for Rho GTPase. These findings uncover the unexpected general machinery and the divergent regulatory logics for the anchorage of the contractile ring through the anillin/Mid1 family proteins from yeast to humans. PubMed: 25959226DOI: 10.1016/j.devcel.2015.03.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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