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Volume 582, Issue 17, Pages 2501-2507 (23 July 2008)


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Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector-GAP complex

Edited by Gianni Cesareni

Stefan Veltel, Aleksandra Kravchenko, Shehab Ismail, Alfred WittinghoferCorresponding Author Informationemail address

Received 7 May 2008; received in revised form 9 May 2008; accepted 13 May 2008. published online 26 June 2008.

Abstract 

Arl2 and Arl3, members of the Arf subfamily of small G proteins, are believed to be involved in ciliary and microtubule-dependent processes. Recently, we could identify RP2, responsible for a variant of X-linked retinitis pigmentosa, as the Arl3-specific GAP. Here, we have characterized Arl2/3 interactions. We show the formation of a ternary complex between Arl3, its cognate GAP RP2 and its retinal effector HRG4. This complex seems to be important for photoreceptor function.

Structured summary


MINT-6602303:

ARL2 (uniprotkb:P36404) binds (MI:0407) to HRG4 (uniprotkb:Q13432) by pull down (MI:0096)

MINT-6602333:

ARL3 (uniprotkb:P36405) binds (MI:0407) to CoD (uniprotkb:Q9BTW9) by pull down (MI:0096)

MINT-6602347, MINT-6602369:

RP2 (uniprotkb:O75695), ARL3 (uniprotkb:P36405) and HRG4 (uniprotkb:Q13432) physically interact (MI:0218) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602195:

PDE delta (uniprotkb:O43924) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602213:

BART (uniprotkb:Q8WZ55) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602239:

ARL3 (uniprotkb:P36405) and BART (uniprotkb:Q8WZ55) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602322:

ARL2 (uniprotkb:P36404) binds (MI:0407) to CoD (uniprotkb:Q9BTW9) by pull down (MI:0096)

MINT-6602258:

RP2 (uniprotkb:Q8IWN7) and ARL3 (uniprotkb:P36405) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602233:

ARL3 (uniprotkb:P36405) and HRG4 (uniprotkb:Q13432) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602360:

HRG4 (uniprotkb:Q13432), ARL3 (uniprotkb:P36405) and RP2 (uniprotkb:O75695) physically interact (MI:0218) by molecular sieving (MI:0071)

MINT-6602297:

ARL2 (uniprotkb:P36404) binds (MI:0407) to PDE delta (uniprotkb:O43924) by pull down (MI:0096)

MINT-6602227:

ARL3 (uniprotkb:P36405) and PDE delta (uniprotkb:O43924) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

MINT-6602204:

HRG4 (uniprotkb:Q13432) and ARL2 (uniprotkb:P36404) bind (MI:0407) by fluorescence polarization spectroscopy (MI:0053)

Max-Planck-Institut für molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany

Corresponding Author InformationCorresponding author.

PII: S0014-5793(08)00550-4

doi:10.1016/j.febslet.2008.05.053


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