Rod disc renewal occurs by evagination of the ciliary plasma membrane that makes cadherin-based contacts with the inner segment. Burgoyne, T., Meschede, I. P., Burden, J. J., Bailly, M., Seabra, M. C., & Futter, C. E. Proceedings of the National Academy of Sciences of the United States of America, 112(52):15922–15927, December, 2015. doi abstract bibtex The outer segments of vertebrate rod photoreceptors are renewed every 10 d. Outer segment components are transported from the site of synthesis in the inner segment through the connecting cilium, followed by assembly of the highly ordered discs. Two models of assembly of discrete discs involving either successive fusion events between intracellular rhodopsin-bearing vesicles or the evagination of the plasma membrane followed by fusion of adjacent evaginations have been proposed. Here we use immuno-electron microscopy and electron tomography to show that rhodopsin is transported from the inner to the outer segment via the ciliary plasma membrane, subsequently forming successive evaginations that "zipper" up proximally, but at their leading edges are free to make junctions containing the protocadherin, PCDH21, with the inner segment plasma membrane. Given the physical dimensions of the evaginations, coupled with likely instability of the membrane cortex at the distal end of the connecting cilium, we propose that the evagination occurs via a process akin to blebbing and is not driven by actin polymerization. Disassembly of these junctions is accompanied by fusion of the leading edges of successive evaginations to form discrete discs. This fusion is topologically different to that mediated by the membrane fusion proteins, SNAREs, as initial fusion is between exoplasmic leaflets, and is accompanied by gain of the tetraspanin rim protein, peripherin.
@article{burgoyne_rod_2015,
title = {Rod disc renewal occurs by evagination of the ciliary plasma membrane that makes cadherin-based contacts with the inner segment},
volume = {112},
issn = {1091-6490},
doi = {10.1073/pnas.1509285113},
abstract = {The outer segments of vertebrate rod photoreceptors are renewed every 10 d. Outer segment components are transported from the site of synthesis in the inner segment through the connecting cilium, followed by assembly of the highly ordered discs. Two models of assembly of discrete discs involving either successive fusion events between intracellular rhodopsin-bearing vesicles or the evagination of the plasma membrane followed by fusion of adjacent evaginations have been proposed. Here we use immuno-electron microscopy and electron tomography to show that rhodopsin is transported from the inner to the outer segment via the ciliary plasma membrane, subsequently forming successive evaginations that "zipper" up proximally, but at their leading edges are free to make junctions containing the protocadherin, PCDH21, with the inner segment plasma membrane. Given the physical dimensions of the evaginations, coupled with likely instability of the membrane cortex at the distal end of the connecting cilium, we propose that the evagination occurs via a process akin to blebbing and is not driven by actin polymerization. Disassembly of these junctions is accompanied by fusion of the leading edges of successive evaginations to form discrete discs. This fusion is topologically different to that mediated by the membrane fusion proteins, SNAREs, as initial fusion is between exoplasmic leaflets, and is accompanied by gain of the tetraspanin rim protein, peripherin.},
language = {eng},
number = {52},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
author = {Burgoyne, Thomas and Meschede, Ingrid P. and Burden, Jemima J. and Bailly, Maryse and Seabra, Miguel C. and Futter, Clare E.},
month = dec,
year = {2015},
pmid = {26668363},
pmcid = {PMC4702997},
keywords = {Animals, Cadherins, Cell Membrane, Cryoelectron Microscopy, Electron Microscope Tomography, Eye, Eye Proteins, Mice, Inbred C57BL, Microscopy, Immunoelectron, Munc18 Proteins, Nerve Tissue Proteins, Photoreceptor Cells, Qa-SNARE Proteins, Retinal Photoreceptor Cell Inner Segment, Retinal Rod Photoreceptor Cells, Rhodopsin, Rod Cell Outer Segment, disc renewal, protocadherin, rhodopsin, rod photoreceptors},
pages = {15922--15927}
}
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Two models of assembly of discrete discs involving either successive fusion events between intracellular rhodopsin-bearing vesicles or the evagination of the plasma membrane followed by fusion of adjacent evaginations have been proposed. Here we use immuno-electron microscopy and electron tomography to show that rhodopsin is transported from the inner to the outer segment via the ciliary plasma membrane, subsequently forming successive evaginations that \"zipper\" up proximally, but at their leading edges are free to make junctions containing the protocadherin, PCDH21, with the inner segment plasma membrane. Given the physical dimensions of the evaginations, coupled with likely instability of the membrane cortex at the distal end of the connecting cilium, we propose that the evagination occurs via a process akin to blebbing and is not driven by actin polymerization. Disassembly of these junctions is accompanied by fusion of the leading edges of successive evaginations to form discrete discs. This fusion is topologically different to that mediated by the membrane fusion proteins, SNAREs, as initial fusion is between exoplasmic leaflets, and is accompanied by gain of the tetraspanin rim protein, peripherin.","language":"eng","number":"52","journal":"Proceedings of the National Academy of Sciences of the United States of America","author":[{"propositions":[],"lastnames":["Burgoyne"],"firstnames":["Thomas"],"suffixes":[]},{"propositions":[],"lastnames":["Meschede"],"firstnames":["Ingrid","P."],"suffixes":[]},{"propositions":[],"lastnames":["Burden"],"firstnames":["Jemima","J."],"suffixes":[]},{"propositions":[],"lastnames":["Bailly"],"firstnames":["Maryse"],"suffixes":[]},{"propositions":[],"lastnames":["Seabra"],"firstnames":["Miguel","C."],"suffixes":[]},{"propositions":[],"lastnames":["Futter"],"firstnames":["Clare","E."],"suffixes":[]}],"month":"December","year":"2015","pmid":"26668363","pmcid":"PMC4702997","keywords":"Animals, Cadherins, Cell Membrane, Cryoelectron Microscopy, Electron Microscope Tomography, Eye, Eye Proteins, Mice, Inbred C57BL, Microscopy, Immunoelectron, Munc18 Proteins, Nerve Tissue Proteins, Photoreceptor Cells, Qa-SNARE Proteins, Retinal Photoreceptor Cell Inner Segment, Retinal Rod Photoreceptor Cells, Rhodopsin, Rod Cell Outer Segment, disc renewal, protocadherin, rhodopsin, rod photoreceptors","pages":"15922–15927","bibtex":"@article{burgoyne_rod_2015,\n\ttitle = {Rod disc renewal occurs by evagination of the ciliary plasma membrane that makes cadherin-based contacts with the inner segment},\n\tvolume = {112},\n\tissn = {1091-6490},\n\tdoi = {10.1073/pnas.1509285113},\n\tabstract = {The outer segments of vertebrate rod photoreceptors are renewed every 10 d. 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Given the physical dimensions of the evaginations, coupled with likely instability of the membrane cortex at the distal end of the connecting cilium, we propose that the evagination occurs via a process akin to blebbing and is not driven by actin polymerization. Disassembly of these junctions is accompanied by fusion of the leading edges of successive evaginations to form discrete discs. 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