Liprin-α and Assembly of the Synaptic Cytomatrix ☆
| Autor: | David Van Vactor, Kyle E. Miller, Vivian T. Chou |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Scaffold protein Chemistry Protein subunit Glutamate receptor Protein phosphatase 2 Cell biology Synapse 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology 0302 clinical medicine Axoplasmic transport CASK Neurotransmitter 030217 neurology & neurosurgery |
| Popis: | Liprin-α is required for synaptic assembly and function. It localizes to multiple classes of synapse, controls the form and function of active zones, regulates axonal transport, targeting of glutamate receptors in dendrites, evoked neurotransmitter release, and is required for normal locomotion and egg laying behavior. Liprin-α interacts with itself and numerous other classes of protein: Liprin−β, Liprin−γ, LAR, PTPσ, PTPδ, APC/C, CASK, ELKS/CAST/ERC, GIT, GRIP, ING4, kinesin-1, kinesin-3, kinesin-4, mDia, NAB-1, PP2A regulatory subunit B, RIM1, and SYD-1/mSYD1A. With the exception of kinesin-4 and ING, these all appear to be involved in normal synaptic function, which suggests Liprin-α acts as a scaffolding protein vital for delivery and assembly of the synaptic cytomatrix. Liprin-α has also been shown to function in axonal transport, a function which may or may not be distinct from its role as a synaptic scaffold. Liprin-α also has diverse roles in non-neuronal contexts. Structurally, Liprin-α is composed of N-terminal coiled-coils and three C-terminal sterile alpha motifs. These structural elements are essential to the interactions between Liprin-α and its wide variety of binding partners. This observation that Liprin-α is primarily composed of protein–protein interaction domains reflects its function as scaffold protein and in cell–cell interactions. |
| Databáze: | OpenAIRE |
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