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Interactions between Transport Protein Particle (TRAPP) complexes and Rab GTPases in Arabidopsis.
Plant J. 100, 279-297 (2019)
Transport Protein Particle II (TRAPPII) is essential for exocytosis, endocytosis, protein sorting and cytokinesis. In spite of a considerable understanding of its biological role, little information is known about Arabidopsis TRAPPII complex topology and molecular function. In this study, independent proteomic approaches initiated with TRAPP components or Rab-A GTPase variants converge on the TRAPPII complex. We show that the Arabidopsis genome encodes the full complement of 13 TRAPPC subunits, including four previously unidentified components. A dimerization model is proposed to account for binary interactions between TRAPPII subunits. Preferential binding to dominant negative (GDP-bound) versus wild-type or constitutively active (GTP-bound) RAB-A2a variants discriminates between TRAPPII and TRAPPIII subunits and shows that Arabidopsis complexes differ from yeast but resemble metazoan TRAPP complexes. Analyzes of Rab-A mutant variants in trappii backgrounds provide genetic evidence that TRAPPII functions upstream of RAB-A2a, allowing us to propose that TRAPPII is likely to behave as a guanine nucleotide exchange factor (GEF) for the RAB-A2a GTPase. GEFs catalyze exchange of GDP for GTP; the GTP-bound, activated, Rab then recruits a diverse local network of Rab effectors to specify membrane identity in subsequent vesicle fusion events. Understanding GEF-Rab interactions will be crucial to unravel the co-ordination of plant membrane traffic.
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Publikationstyp
Artikel: Journalartikel
Dokumenttyp
Wissenschaftlicher Artikel
Schlagwörter
Arabidopsis Thaliana ; Cytokinesis ; Rab Gtpases ; Secretory Pathway ; Tethering Complexes; Nucleotide Exchange Factor; Bovine Brain Cytosol; Golgi Network; Regulates Autophagy; Subsequent Binding; Sequential Action; Plasma-membrane; Cytokinesis; Trafficking; Gene
ISSN (print) / ISBN
0960-7412
e-ISSN
1365-313X
Zeitschrift
Plant Journal, The
Quellenangaben
Band: 100,
Heft: 2,
Seiten: 279-297
Verlag
Wiley
Verlagsort
111 River St, Hoboken 07030-5774, Nj Usa
Nichtpatentliteratur
Publikationen
Begutachtungsstatus
Peer reviewed
Institut(e)
Institute of Network Biology (INET)