Synapsin I senses membrane curvature by an amphipathic lipid packing sensor motif

Ludwig Krabben, Anna Fassio, Vikram Kjoller Bhatia, Arndt Pechstein, Franco Onofri, Manuela Fadda, Mirko Messa, Yijian Rao, Oleg Shupliakov, Dimitrios Stamou, Fabio Benfenati, Volker Haucke

Результат исследований: Научные публикации в периодических изданияхстатьярецензирование

27 Цитирования (Scopus)

Аннотация

Sustained neurotransmitter release at synapses during high-frequency synaptic activity involves the mobilization of synaptic vesicles (SVs) from the tightly clustered reserve pool (RP). Synapsin I (Syn I), a brain-specific peripheral membrane protein that undergoes activity-dependent cycles of SV association and dissociation, is implicated in RP organization via its ability to cluster SVs. Although Syn I has affinity for phospholipids, the mechanism for the reversible association of synapsin with SV membranes remains enigmatic. Here, we show that rat Syn I is able to sense membrane curvature via an evolutionary conserved amphipathic lipid packing sensor motif(ALPS). Deletion or mutational inactivation of the ALPS impairs the ability of Syn I to associate with highly curved membranes and with SVs. Furthermore, a Syn I mutant lacking ALPS displays defects in its ability to undergo activity-induced cycles of dispersion and reclustering in neurons and fails to induce vesicle clustering in vitro. Our data suggest a crucial role for ALPS-mediated sensing of membrane curvature in regulating synapsin function.

Язык оригиналаанглийский
Страницы (с-по)18149-18154
Число страниц6
ЖурналJournal of Neuroscience
Том31
Номер выпуска49
DOI
СостояниеОпубликовано - 7 дек 2011

Предметные области Scopus

  • Нейробиология (все)

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