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the extended synaptotagmins (E-Syts), endoplasmic reticulum (ER) proteins that function as PtdIns(4,5)P2- and Ca(2 (zeige CA2 Proteine)+)-regulated tethers to the Pplasma membrane.
SYT2 mutations cause a novel complex presynaptic congenital myasthenic syndrome characterized by motor neuropathy causing lower limb wasting and foot deformities, reflex potentiation following exercise and a prolonged period of posttetanic potentiation
Synaptotagmin 2 mutations cause an autosomal-dominant form of lambert-eaton myasthenic syndrome and nonprogressive motor neuropathy.
Human SytII is not an effective receptor for Botulinum neurotoxin D-C.
synaptotagmin-II is not a high affinity receptor for BoNT/B and G due to a phenylalanine to leucine mutation in its luminal domain present only in humans and chimpanzees
role for synaptotagmin II as calcium-sensor during phagocytosis and secretion in neutrophils
both synaptotagmins I and II can interact with the syntaxin/synaptosomal-associated protein of 25 kDa (SNAP-25 (zeige SNAP25 Proteine)) dimer
WNK1 (zeige WNK1 Proteine) selectively binds to and phosphorylates synaptotagmin 2 (Syt2) within its calcium binding C2 domains. Endogenous WNK1 (zeige WNK1 Proteine) and Syt2 coimmunoprecipitate and colocalize on a subset of secretory granules in INS-1 (zeige FOXM1 Proteine) cells.
A recombinant fragment from the luminal domain of the human receptor protein syt (zeige SS18 Proteine) II can bind specifically to botulinum neurotoxin B and its Hc domain.
Mutation of overexpressed Syt2 transgene leaves intrinsic calcium sensitivity of vesicles intact while it destabilizes the readily releasable pool of vesicles and loosens the tight coupling between calcium influx and release.
Authors propose that the strong reduction of Syt2 and SV2B (zeige SV2B Proteine) are key factors of the functional synaptic alteration and that the physiological downregulation of Syt1 (zeige SYT1 Proteine) plays a determinant role in muscle vulnerability in SMA (zeige SMN1 Proteine)
Deletion of Syt2 severely reduced and delayed disynaptic inhibition following parallel fiber stimulation and as release sensor at GABAergic basket cell-Purkinje cell synapses ensures fast and efficient feedforward inhibition in cerebellar microcircuit.
aM inhibitors or the inhibition of the Ca(2 (zeige CA2 Proteine)+)-calmodulin-Munc13-1 signaling pathway only impaired the uptake of Syt2 while leaving membrane retrieval intact, indicating different recycling mechanisms for membranes and vesicle proteins. Our data identify a novel mechanism of stimulus- and Ca(2 (zeige CA2 Proteine)+)-dependent regulation of coordinated endocytosis of synaptic membranes and vesicle proteins.
we identify Syt2 as a functionally important Ca(2 (zeige CA2 Proteine)+) sensor at fast-releasing inhibitory synapses, and show that Syt1 (zeige SYT1 Proteine) and Syt2 can redundantly control transmitter release at specific brain synapses
demonstrates a developmental Syt1 (zeige SYT1 Proteine)-Syt2 isoform switch at an identified synapse, a mechanism that could fine-tune the speed, reliability, and plasticity of transmitter release at fast releasing CNS synapses.
the combined inactivation of all 3 E-Syt (zeige SS18 Proteine) genes has no effect on mouse viability or fertility.
The 2.3-A structure of a ternary complex of botulinum neurotoxin type B bound to both its protein receptor synaptotagmin II and its ganglioside receptor GD1a, is reported.
Synaptotagmins 1 and 2 as mediators of rapid exocytosis at nerve terminals: the dyad hypothesis
Syt2 make it an excellent marker for analyzing the development and plasticity of perisomatic inhibitory innervations onto both excitatory and inhibitory neurons in the visual cortex.
Syt2 increases the dynamic range of synapses by driving release with a high Ca(2 (zeige CA2 Proteine))+ cooperativity, as well as by suppressing a remaining, near-linear Ca(2 (zeige CA2 Proteine))+ sensor.
knockdown of synaptotagmin 2 (syt2) reduces synchronous release, whereas knockdown of synaptotagmin 7 (syt7 (zeige SYT7 Proteine)) reduces the asynchronous component of release.
Synaptotagmins, like SYT2, are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis (Hilbush and Morgan, 1994
, synaptotagmin II