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Characterization of the small Arabidopsis thaliana GTPase and ADP-ribosylation factor-like 2 protein TITAN 5.
Mohr, Inga; Mirzaiebadizi, Amin; Sanyal, Sibaji K; Chuenban, Pichaporn; Ahmadian, Mohammad R; Ivanov, Rumen; Bauer, Petra.
Afiliación
  • Mohr I; Institute of Botany, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Mirzaiebadizi A; Institute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Sanyal SK; Institute of Botany, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Chuenban P; Institute of Botany, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Ahmadian MR; Center for Plant Genome Engineering, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Ivanov R; Institute of Biochemistry and Molecular Biology II, Medical Faculty and University Hospital Düsseldorf, Heinrich Heine University, 40225 Düsseldorf, Germany.
  • Bauer P; Institute of Botany, Heinrich Heine University, 40225 Düsseldorf, Germany.
J Cell Sci ; 137(15)2024 08 01.
Article en En | MEDLINE | ID: mdl-39056156
ABSTRACT
Small GTPases switch between GDP- and GTP-bound states during cell signaling. The ADP-ribosylation factor (ARF) family of small GTPases is involved in vesicle trafficking. Although evolutionarily well conserved, little is known about ARF and ARF-like GTPases in plants. We characterized biochemical properties and cellular localization of the essential small ARF-like GTPase TITAN 5 (TTN5; also known as HALLIMASCH, ARL2 and ARLC1) from Arabidopsis thaliana, and two TTN5 proteins with point mutants in conserved residues, TTN5T30N and TTN5Q70L, that were expected to be unable to perform nucleotide exchange and GTP hydrolysis, respectively. TTN5 exhibited very rapid intrinsic nucleotide exchange and remarkably low GTP hydrolysis activity, functioning as a non-classical small GTPase being likely present in a GTP-loaded active form. We analyzed signals from YFP-TTN5 and HA3-TTN5 by in situ immunolocalization in Arabidopsis seedlings and through use of a transient expression system. Colocalization with endomembrane markers and pharmacological treatments suggests that TTN5 can be present at the plasma membrane and that it dynamically associates with membranes of vesicles, Golgi stacks and multivesicular bodies. Although TTN5Q70L mirrored wild-type TTN5 behavior, the TTN5T30N mutant differed in some aspects. Hence, the unusual rapid nucleotide exchange activity of TTN5 is linked with its membrane dynamics, and TTN5 likely has a role in vesicle transport within the endomembrane system.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: J Cell Sci Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: J Cell Sci Año: 2024 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido