4XOI

Structure of hsAnillin bound with RhoA(Q63L) at 2.1 Angstroms resolution

Summary for 4XOI

• Entry DOI: 10.2210/pdb4xoi/pdb
• Related: 4XH3 4XOH
• Descriptor: Transforming protein RhoA, Actin-binding protein anillin, GUANOSINE-5'-TRIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: rhoa-anillin complex, cell cycle
• Biological source: Homo sapiens (Human); More
• Cellular location: Cell membrane; Lipid-anchor; Cytoplasmic side: P61586; Nucleus: Q9NQW6
• Total number of polymer chains: 4
• Total formula weight: 100975.43

Authors

Sun, L.,Guan, R.,Lee, I.-J.,Liu, Y.,Chen, M.,Wang, J.,Wu, J.,Chen, Z. (deposition date: 2015-01-16, 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

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: 25959226
DOI: 10.1016/j.devcel.2015.03.003

Experimental method

X-RAY DIFFRACTION (2.092 Å)