RHOA:GTP:DIAPH1 binds EVL and sequesters profilin:G-actin from MKL1

Stable Identifier
Reaction [binding]
Homo sapiens
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Once activated by binding to RHOA:GTP, DIAPH1 binds profilin:G-actin complexes together with EVL (VASP) homotetramers and promotes elongation of actin filaments (Copeland and Treisman 2002, Grosse et al. 2003, Kursula et al. 2008, Breitsprecher et al. 2008). Binding of nonpolymerized actin (G-actin) to DIAPH1 and EVL releases MKL1 (MAL) transcription co-factor which is inhibited when bound to G-actin (Miralles et al. 2003).

Literature References
PubMed ID Title Journal Year
12805219 A role for VASP in RhoA-Diaphanous signalling to actin dynamics and SRF activity

Treisman, R, Copeland, JW, Grosse, R, Newsome, TP, Way, M

EMBO J. 2003
18923426 Clustering of VASP actively drives processive, WH2 domain-mediated actin filament elongation

Faix, J, Urbanke, C, Breitsprecher, D, Kiesewetter, AK, Resch, GP, Small, JV, Linkner, J

EMBO J. 2008
18001770 High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP

Massimi, M, Wilmanns, M, Downer, J, Kursula, P, Song, YH, Kursula, I, Witke, W, Stanley, WA

J. Mol. Biol. 2008
12429848 The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization

Treisman, R, Copeland, JW

Mol. Biol. Cell 2002
12732141 Actin dynamics control SRF activity by regulation of its coactivator MAL

Posern, G, Treisman, R, Miralles, F, Zaromytidou, AI

Cell 2003
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