Abstract
Photoreceptor retinol dehydrogenase (prRDH) is a membrane-associated cytosolic protein that localizes to the outer segments (OS) of rods and cones. Here, we demonstrate that the C-terminal 16 amino acids of prRDH confer membrane association as well as cone and rod OS targeting on a linked green fluorescent protein. Membrane association in transfected 293 cells and in transgenic Xenopus photoreceptors is mediated by fatty acylation at one or more evolutionarily conserved cysteines within the prRDH C-terminal tail. In bovine OS, native prRDH is similarly acylated, and hydrolysis of this linkage releases the protein from the membrane. Efficient OS localization requires both membrane association and the prRDH sequence ... (V/I)XPX at the extreme C terminus, which closely resembles the C-terminal sequence that targets opsin/rhodopsin to the OS. Taken together, these data imply that the C-terminal ... (V/I)XPX sequence is a general OS localization signal that can function in the context of both integral and peripheral membrane proteins. This strategy for OS localization resembles those used for protein localization to mitochondria, peroxisomes, endosomes, and endoplasmic reticulum; in each case, a short N- or C-terminal sequence is shared among structurally diverse proteins that are targeted to the same subcellular destination.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2623-2632 |
| Number of pages | 10 |
| Journal | Journal of Neuroscience |
| Volume | 24 |
| Issue number | 11 |
| DOIs | |
| State | Published - Mar 17 2004 |
| Externally published | Yes |
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Keywords
- Inner segment
- Outer segment
- Palmitoylation
- Photoreceptor
- Protein sorting
- Retinol dehydrogenase
- Transgenic Xenopus
ASJC Scopus subject areas
- Neuroscience(all)
Cite this
An Outer Segment Localization Signal at the C Terminus of the Photoreceptor-Specific Retinol Dehydrogenase. / Luo, Wenqin; Marsh-Armstrong, Nicholas; Rattner, Amir; Nathans, Jeremy.
In: Journal of Neuroscience, Vol. 24, No. 11, 17.03.2004, p. 2623-2632.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - An Outer Segment Localization Signal at the C Terminus of the Photoreceptor-Specific Retinol Dehydrogenase
AU - Luo, Wenqin
AU - Marsh-Armstrong, Nicholas
AU - Rattner, Amir
AU - Nathans, Jeremy
PY - 2004/3/17
Y1 - 2004/3/17
N2 - Photoreceptor retinol dehydrogenase (prRDH) is a membrane-associated cytosolic protein that localizes to the outer segments (OS) of rods and cones. Here, we demonstrate that the C-terminal 16 amino acids of prRDH confer membrane association as well as cone and rod OS targeting on a linked green fluorescent protein. Membrane association in transfected 293 cells and in transgenic Xenopus photoreceptors is mediated by fatty acylation at one or more evolutionarily conserved cysteines within the prRDH C-terminal tail. In bovine OS, native prRDH is similarly acylated, and hydrolysis of this linkage releases the protein from the membrane. Efficient OS localization requires both membrane association and the prRDH sequence ... (V/I)XPX at the extreme C terminus, which closely resembles the C-terminal sequence that targets opsin/rhodopsin to the OS. Taken together, these data imply that the C-terminal ... (V/I)XPX sequence is a general OS localization signal that can function in the context of both integral and peripheral membrane proteins. This strategy for OS localization resembles those used for protein localization to mitochondria, peroxisomes, endosomes, and endoplasmic reticulum; in each case, a short N- or C-terminal sequence is shared among structurally diverse proteins that are targeted to the same subcellular destination.
AB - Photoreceptor retinol dehydrogenase (prRDH) is a membrane-associated cytosolic protein that localizes to the outer segments (OS) of rods and cones. Here, we demonstrate that the C-terminal 16 amino acids of prRDH confer membrane association as well as cone and rod OS targeting on a linked green fluorescent protein. Membrane association in transfected 293 cells and in transgenic Xenopus photoreceptors is mediated by fatty acylation at one or more evolutionarily conserved cysteines within the prRDH C-terminal tail. In bovine OS, native prRDH is similarly acylated, and hydrolysis of this linkage releases the protein from the membrane. Efficient OS localization requires both membrane association and the prRDH sequence ... (V/I)XPX at the extreme C terminus, which closely resembles the C-terminal sequence that targets opsin/rhodopsin to the OS. Taken together, these data imply that the C-terminal ... (V/I)XPX sequence is a general OS localization signal that can function in the context of both integral and peripheral membrane proteins. This strategy for OS localization resembles those used for protein localization to mitochondria, peroxisomes, endosomes, and endoplasmic reticulum; in each case, a short N- or C-terminal sequence is shared among structurally diverse proteins that are targeted to the same subcellular destination.
KW - Inner segment
KW - Outer segment
KW - Palmitoylation
KW - Photoreceptor
KW - Protein sorting
KW - Retinol dehydrogenase
KW - Transgenic Xenopus
UR - http://www.scopus.com/inward/record.url?scp=1642377058&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=1642377058&partnerID=8YFLogxK
U2 - 10.1523/JNEUROSCI.5302-03.2004
DO - 10.1523/JNEUROSCI.5302-03.2004
M3 - Article
VL - 24
SP - 2623
EP - 2632
JO - Journal of Neuroscience
JF - Journal of Neuroscience
SN - 0270-6474
IS - 11
ER -