Longins and their longin domains: Regulated SNAREs and multifunctional SNARE regulators

Valeria Rossi, David K. Banfield, Marcella Vacca, Lars E P Dietrich, Christian Ungermann, Maurizio D'Esposito, Thierry Galli, Francesco Filippini

Research output: Contribution to journalArticlepeer-review

Abstract

Longins are the only R-SNAREs that are common to all eukaryotes and are characterized by a conserved N-terminal domain with a profilin-like fold called a longin domain (LD). These domains seem to be essential for regulating membrane trafficking and they mediate unexpected biochemical functions via a range of protein-protein and intramolecular binding specificities. In addition to the longins, proteins involved in the regulation of intracellular trafficking, such as subunits of the adaptor and transport protein particle complexes, also have LD-like folds. The functions and cellular localization of longins are regulated at several levels and the longin prototypes TI-VAMP, Sec22 and Ykt6 show different distributions among eukaryotes, reflecting their modular and functional diversity. In mammals, TI-VAMP and Ykt6 are crucial for neuronal function, and defects in longin structure or function might underlie some human neurological pathologies.

Original languageEnglish
Pages (from-to)682-688
Number of pages7
JournalTrends in Biochemical Sciences
Volume29
Issue number12
DOIs
Publication statusPublished - Dec 2004

ASJC Scopus subject areas

  • Biochemistry

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