Ca2+-sensor for vesicle exocytosis
|
a protein capable to trigger exocytosis upon binding of calcium ions (Ca2+), but unable to fuse membranes in the absence of proteins—fusogenes. |
Synaptic vesicle (SV) tethering
|
primary recruitment of SV to the active zone. |
SV docking
|
tighter attachment of SV to the membrane than tethering. |
SV priming
|
the sequence of events rendering a SV competent for exocytosis. |
Inner ear
|
innermost part of the vertebrate ear, responsible for hearing (cochlea) and sense of balance (vestibular system: semicircular canals, utricle and saccule). |
Hair cells
|
cells characterized by a hair bundle and ability to sense and amplify mechanical stimuli (the outer hair cells (OHCs) of the mammalian cochlea) or transducing the latter into chemical signals (e.g., the inner hair cells (IHCs) of the mammalian cochlea). Hair cells are found in the inner ear and in the lateral line of vertebrates. |
Lateral line
|
a system of sense organs found in aquatic vertebrates, detecting movement and pressure gradients of surrounding water. |
Rhabdomyosarcoma
|
rare, aggressive and malignant pediatric skeletal muscle cancer of immature muscle cells. |
Ribbon synapse
|
synapse characterized by presence of a ribbon—presynaptic electron-dense body build up by several scaffolding proteins, tethering a halo of SVs and necessary to, e.g., support large readily releasable pool of SVs. |
Sarcolemma
|
surface membrane limiting striated (skeletal and cardiac) muscle fibers. |
T-tubules
|
system of transverse tubular extensions of sarcolemma penetrating the interior of striated myofibers and important for propagation of action potentials and synchronization of the fibers’ contraction. |
Triad
|
constitutes the anatomical basis for excitation-contraction coupling in striated muscle fibers and is formed by one T-tubule in the middle and two terminal cisternae of sarcoplasmic reticulum contacting it from both sides. |
A/J mice
|
mouse model of dysferlinopathy, carrying an ETn retrotransposon insertion in intron 4 of Dysf, which results in the complete lack of dysferlin expression. |
SJL/J mice
|
mouse model of dysferlinopathy characterized by residual expression of dysferlin carrying a 57 amino acids deletion in the C2E domain due to a splice site mutation in exon 45. |