Abstract:
:RhoA stimulates cell contractility by recruiting downstream effectors to the cortical plasma membrane. We now show that direct binding by anillin is required for effective signaling: this antagonizes the otherwise labile membrane association of GTP-RhoA to promote effector recruitment. However, since its binding to RhoA blocks access by other effectors, we demonstrate that anillin must also concentrate membrane phosphoinositide-4,5-P2 (PIP2) to promote signaling. We propose and test a sequential pathway where GTP-RhoA first binds to anillin and then is retained at the membrane by PIP2 after it disengages from anillin. Importantly, re-binding of membrane GTP-RhoA to anillin, regulated by the cortical density of anillin, creates cycles through this pathway. These cycles repeatedly reset the dissociation kinetics of GTP-RhoA, substantially increasing its dwell time to recruit effectors. Thus, anillin regulates RhoA signaling by a paradigm of kinetic scaffolding that may apply to other signals whose efficacy depends on their cortical dwell times.
journal_name
Dev Celljournal_title
Developmental cellauthors
Budnar S,Husain KB,Gomez GA,Naghibosadat M,Varma A,Verma S,Hamilton NA,Morris RG,Yap ASdoi
10.1016/j.devcel.2019.04.031subject
Has Abstractpub_date
2019-06-17 00:00:00pages
894-906.e12issue
6eissn
1534-5807issn
1878-1551pii
S1534-5807(19)30328-4journal_volume
49pub_type
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