A human exchange factor for ARF contains Sec-7- and pleckstrin-homology domains

Article Abstract:

The human protein, ARNO, includes Sec7 and carboxy-terminal pleckstrin-homology (PH) domains stimulating guanine-nucleotide exchange on ARF1. The PH domain uses the negatively charged phospholipid vesicles supplemented with phosphatidylinositol biphosphate to mediate an increase in the ARNO exchange activity. Brefeldin A fails to suppress the exchange activity of ARNO. This reveals the presence of a regulatory component, associating with ARNO, which is sensitive to brefeldin A.

Physiological aspects, G proteins, Phosphoinositides, Phosphatidylinositols

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Structure of the Sec 7 domain of the Arf exchange factor ARNO

Article Abstract:

Small G proteins change from a resting to an active GDP-bound state. Guanine-nucleotide-exchange factors are needed to encourage fast activation of small G proteins by replacing them with GTP 'in vivo'. This process encourages 'the coating of secretory vesicles in Golgi traffic'. An exchange factor and two other proteins have been identified. They have a central Sec7-like domain which houses the exchange-factor. The crystal structure of the Sec7 domain has been observed.

Research and Development in the Physical, Engineering, and Life Sciences, Molecular Biology, Research, Biochemistry, Proteins

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