[HTML][HTML] The role of α-synuclein in SNARE-mediated synaptic vesicle fusion
Neuronal communication depends on exquisitely regulated membrane fusion between
synaptic vesicles and presynaptic neurons, which results in neurotransmitter release in …
synaptic vesicles and presynaptic neurons, which results in neurotransmitter release in …
Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin
Synaptic vesicle (SV) exocytosis is mediated by SNARE proteins. Reconstituted SNAREs
are constitutively active, so a major focus has been to identify fusion clamps that regulate …
are constitutively active, so a major focus has been to identify fusion clamps that regulate …
Regulation of exocytotic fusion pores by SNARE protein transmembrane domains
Z Wu, S Thiyagarajan, B O'Shaughnessy… - Frontiers in Molecular …, 2017 - frontiersin.org
Calcium-triggered exocytotic release of neurotransmitters and hormones from neurons and
neuroendocrine cells underlies neuronal communication, motor activity and endocrine …
neuroendocrine cells underlies neuronal communication, motor activity and endocrine …
α-Synuclein may cross-bridge v-SNARE and acidic phospholipids to facilitate SNARE-dependent vesicle docking
Misfolded α-synuclein (A-syn) is widely recognized as the primal cause of
neurodegenerative diseases including Parkinson's disease and dementia with Lewy bodies …
neurodegenerative diseases including Parkinson's disease and dementia with Lewy bodies …
Synaptotagmin-1 binds to PIP2-containing membrane but not to SNAREs at physiological ionic strength
Abstract The Ca2+ sensor synaptotagmin-1 is thought to trigger membrane fusion by binding
to acidic membrane lipids and SNARE proteins. Previous work has shown that binding is …
to acidic membrane lipids and SNARE proteins. Previous work has shown that binding is …
Synaptotagmin-1 membrane binding is driven by the C2B domain and assisted cooperatively by the C2A domain
Synaptotagmin interaction with anionic lipid (phosphatidylserine/phosphatidylinositol)
containing membranes, both in the absence and presence of calcium ions (Ca2+), is critical …
containing membranes, both in the absence and presence of calcium ions (Ca2+), is critical …
Ring-like oligomers of Synaptotagmins and related C2 domain proteins
We recently reported that the C2AB portion of Synaptotagmin 1 (Syt1) could self-assemble
into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate …
into Ca2+-sensitive ring-like oligomers on membranes, which could potentially regulate …
Synaptotagmin-1 C2B domains cooperatively stabilize the fusion stalk via a master-servant mechanism
Synaptotagmin-1 is a low-affinity Ca2+ sensor that triggers synchronous vesicle fusion. It
contains two similar C2 domains (C2A and C2B) that cooperate in membrane binding, being …
contains two similar C2 domains (C2A and C2B) that cooperate in membrane binding, being …
Human transposons are an abundant supply of transcription factor binding sites and promoter activities in breast cancer cell lines
Background Transposable elements (TE) are commonly regarded as “junk DNA” with no
apparent regulatory roles in the human genome. However, a growing body of evidence …
apparent regulatory roles in the human genome. However, a growing body of evidence …
The synaptotagmin-1 C2B domain is a key regulator in the stabilization of the fusion pore
Fusion pores serve as an effective mechanism to connect intracellular organelles and
release vesicle contents during exocytosis. A complex lipid rearrangement takes place as …
release vesicle contents during exocytosis. A complex lipid rearrangement takes place as …