D
IPR013912

Adenylate cyclase-associated CAP, C-terminal

InterPro entry
Short nameAdenylate_cyclase-assoc_CAP_C
Overlapping
homologous
superfamilies
 
domain relationships

Description

Cyclase-associated proteins (CAPs) are highly conserved actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways
[2, 3, 4, 5]
. In Drosophila, CAP functions in Hedgehog-mediated eye development and in establishing oocyte polarity. In Dictyostelium (slim mold), CAP is involved in microfilament reorganisation near the plasma membrane in a PIP2-regulated manner and is required to perpetuate the cAMP relay signal to organise fruitbody formation. In plants, CAP is involved in plant signalling pathways required for co-ordinated organ expansion. In yeast, CAP is involved in adenylate cyclase activation, as well as in vesicle trafficking and endocytosis. In both yeast and mammals, CAPs appear to be involved in recycling G-actin monomers from ADF/cofilins for subsequent rounds of filament assembly
[6, 7]
. In mammals, there are two different CAPs (CAP1 and CAP2) that share 64% amino acid identity.

This entry represents the C-terminal domain of CAP proteins, which is responsible for G-actin-binding. This domain has a superhelical structure, where the superhelix turns are made of two β-strands each
[1]
.

References

1.Crystal structure of the actin binding domain of the cyclase-associated protein. Dodatko T, Fedorov AA, Grynberg M, Patskovsky Y, Rozwarski DA, Jaroszewski L, Aronoff-Spencer E, Kondraskina E, Irving T, Godzik A, Almo SC. Biochemistry 43, 10628-41, (2004). View articlePMID: 15311924

2.Cyclase-associated proteins: CAPacity for linking signal transduction and actin polymerization. Hubberstey AV, Mottillo EP. FASEB J. 16, 487-99, (2002). View articlePMID: 11919151

3.Arabidopsis CAP1 - a key regulator of actin organisation and development. Deeks MJ, Rodrigues C, Dimmock S, Ketelaar T, Maciver SK, Malho R, Hussey PJ. J. Cell. Sci. 120, 2609-18, (2007). View articlePMID: 17635992

4.Mammalian homolog of the yeast cyclase associated protein, CAP/Srv2p, regulates actin filament assembly. Freeman NL, Field J. Cell Motil. Cytoskeleton 45, 106-20, (2000). View articlePMID: 10658207

5.Crystallization of cyclase-associated protein from Dictyostelium discoideum. Hofmann A, Hess S, Noegel AA, Schleicher M, Wlodawer A. Acta Crystallogr. D Biol. Crystallogr. 58, 1858-61, (2002). View articlePMID: 12351838

6.Mechanism and biological role of profilin-Srv2/CAP interaction. Bertling E, Quintero-Monzon O, Mattila PK, Goode BL, Lappalainen P. J. Cell. Sci. 120, 1225-34, (2007). View articlePMID: 17376963

7.Cyclase-associated protein 1 (CAP1) promotes cofilin-induced actin dynamics in mammalian nonmuscle cells. Bertling E, Hotulainen P, Mattila PK, Matilainen T, Salminen M, Lappalainen P. Mol. Biol. Cell 15, 2324-34, (2004). View articlePMID: 15004221

Further reading

8. Association of yeast adenylyl cyclase with cyclase-associated protein CAP forms a second Ras-binding site which mediates its Ras-dependent activation. Shima F, Okada T, Kido M, Sen H, Tanaka Y, Tamada M, Hu CD, Yamawaki-Kataoka Y, Kariya K, Kataoka T. Mol. Cell. Biol. 20, 26-33, (2000). View articlePMID: 10594005

GO terms

molecular function

cellular component

  • None
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