Otoferlin is a calcium sensor that directly regulates SNARE-mediated membrane fusion

Characterization of Lipid Binding Specificities of Dysferlin C2 Domains Reveals Novel Interactions with Phosphoinositides†

(2009) Christian Therrien et al.   BIOCHEMISTRY

Synaptotagmin-Mediated Bending of the Target Membrane Is a Critical Step in Ca2+-Regulated Fusion

(2009) Enfu Hui et al.   CELL

Otoferlin interacts with myosin VI: implications for maintenance of the basolateral synaptic structure of the inner hair cell

(2009) P. Heidrych et al.   HUMAN MOLECULAR GENETICS

How Does Synaptotagmin Trigger Neurotransmitter Release?

(2008) Edwin R. Chapman   Annual Review of Biochemistry

Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form

(2008) P. Heidrych et al.   HUMAN MOLECULAR GENETICS

Direct Interaction of Otoferlin with Syntaxin 1A, SNAP-25, and the L-type Voltage-gated Calcium Channel CaV1.3

(2008) Neeliyath A. Ramakrishnan et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Synaptotagmin C2B Domain Regulates Ca2+-triggered Fusionin Vitro

(2008) Jon D. Gaffaney et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Evidence That Vesicles Undergo Compound Fusion on the Synaptic Ribbon

(2008) G. Matthews et al.   JOURNAL OF NEUROSCIENCE

Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+

(2008) Michael C Chicka et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

The Janus-faced nature of the C2B domain is fundamental for synaptotagmin-1 function

(2008) Mingshan Xue et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY