Control of eukaryotic membrane fusion by N-terminal domains of SNARE proteins.
SNARE proteins function at the center of membrane fusion reactions by forming complexes with each other via their coiled-coil domains. Several SNAREs have N-terminal domains (NTDs) that precede the coiled-coil domain and have critical functions in regulating the fusion cascade. This review will highlight recent findings on NTDs of syntaxins, the longin domain of VAMP proteins and SNAP-23/25 homologues in yeast. Biochemical and genetic experiments as well as the resolution of several NMR and crystal structures of SNARE NTDs shed light on their diverse function.
Dietrich
Lars E P
LE
Biochemie Zentrum Heidelberg (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120, Heidelberg, Germany. cu2@ix.urz.uni-heidelberg.de
Boeddinghaus
Christine
C
LaGrassa
Tracy J
TJ
Ungermann
Christian
C
D000818:Animals; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D050600:SNARE Proteins; D013329:Structure-Activity Relationship; D033921:Vesicular Transport Proteins
D008565:Membrane Proteins; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins