Premium
Regulation of ADL6 activity by its associated molecular network
Author(s) -
Lam Bernard C.H.,
Sage Tammy L.,
Bianchi Fabrizio,
Blumwald Eduardo
Publication year - 2002
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.2002.01377.x
Subject(s) - dynamin , clathrin , gtpase , clathrin adaptor proteins , vesicle , microbiology and biotechnology , golgi apparatus , biology , signal transducing adaptor protein , interactome , sh3 domain , arabidopsis , vesicular transport protein , proto oncogene tyrosine protein kinase src , endocytosis , biochemistry , receptor , signal transduction , gene , membrane , endoplasmic reticulum , mutant
Summary Plant dynamin‐like proteins consist of a group of high molecular weight GTPase with diverse structural arrangements and cellular localizations. In addition, unlike animal dynamins, there was no evidence for the involvement of any plant dynamin‐like protein in clathrin‐mediated vesicle trafficking. In this study we demonstrate that ADL6 ( Arabidopsis dynamin‐like protein 6), due to its domain arrangement, behaves similarly to the animal dynamins. The association of ADL6 with clathrin‐coated vesicles was demonstrated by co‐fractionation and immunocytochemical studies. ADL6 also interacted via its C‐terminus with γ‐adaptin, an adaptor protein of clathrin‐coated vesicles. Our results suggest that ADL6 participates in clathrin‐mediated vesicle trafficking originating from the Golgi. In addition, our studies demonstrate that ADL6 intrinsic GTPase activity is regulated by its association with acidic phospholipids and an SH3 (Src homology 3)‐containing protein.