Ribeye protein is intrinsically dynamic but is stabilized in the context of the ribbon synapse.

Ribeye protein is intrinsically dynamic but is stabilized in the context of the ribbon synapse.

J Physiol. 2017 Oct 31;:

Authors: Chen Z, Chou SW, McDermott BM

Abstract
Ribeye protein is a major constituent of the synaptic ribbon, an organelle that coordinates rapid and sustained vesicle release to enable hearing and balance. The ribbon is considered to be a stable structure. However, under certain physiological conditions such as acoustic overexposure that results in temporary noise-induced hearing loss or perturbations of ion channels, ribbons may change shape or vanish altogether, suggesting greater plasticity than previously appreciated. The dynamic properties of ribeye proteins are unknown. Here we use transgenesis and imaging to explore the behaviours of ribeye proteins within the ribbon and also their intrinsic properties outside the context of the ribbon synapse in a control cell type, the skin cell. By fluorescence recovery after photobleaching (FRAP) on transgenic zebrafish larvae, we test whether ribeye proteins are dynamic in vivo in real time. In the skin, a cell type devoid of synaptic contacts, Ribeye a-mCherry exchanges with ribbon-like structures on a minute timescale (t1/2  = 3.2 min). In contrast, Ribeye a of the ear and lateral line and Ribeye b of the lateral line each exchange at ribbons of hair cells an order of magnitude slower (t1/2 of 125.6 min, 107.0 min, and 95.3 min, respectively) than Ribeye a of the skin. These basal exchange rates suggest that long-term ribbon presence may require ribeye renewal. Our studies demonstrate that ribeye proteins are inherently dynamic but are stabilized at the ribbons of sensory cells in vivo. This article is protected by copyright. All rights reserved.

PMID: 29086422 [PubMed - as supplied by publisher]

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