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XB-ART-56349
J Cell Biol January 1, 2019; 218 (11): 3753-3772.
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An intrinsic compartmentalization code for peripheral membrane proteins in photoreceptor neurons.

Maza NA , Schiesser WE , Calvert PD .


Abstract
In neurons, peripheral membrane proteins are enriched in subcellular compartments, where they play key roles, including transducing and transmitting information. However, little is known about the mechanisms underlying their compartmentalization. To explore the roles of hydrophobic and electrostatic interactions, we engineered probes consisting of lipidation motifs attached to fluorescent proteins by variously charged linkers and expressed them in Xenopus rod photoreceptors. Quantitative live cell imaging showed dramatic differences in distributions and dynamics of the probes, including presynapse and ciliary OS enrichment, depending on lipid moiety and protein surface charge. Opposing extant models of ciliary enrichment, most probes were weakly membrane bound and diffused through the connecting cilium without lipid binding chaperone protein interactions. A diffusion-binding-transport model showed that ciliary enrichment of a rhodopsin kinase probe occurs via recycling as it perpetually leaks out of the ciliary OS. The model accounts for weak membrane binding of peripheral membrane proteins and a leaky connecting cilium diffusion barrier.

PubMed ID: 31594805
PMC ID: PMC6829649
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: akap13 cps1 dbt dcc grk1 mtor rho


Article Images: [+] show captions
References [+] :
Baehr, Membrane protein transport in photoreceptors: the function of PDEδ: the Proctor lecture. 2015, Pubmed