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| summary_text = RRBP1 is a membrane-bound protein found in the [[endoplasmic reticulum]] (ER). It was originally identified as the ribosome receptor for the ER,<ref name="SavitzMeyer1990">{{cite journal|last1=Savitz|first1=Adam J.|last2=Meyer|first2=David I.|title=Identification of a ribosome receptor in the rough endoplasmic reticulum|journal=Nature|volume=346|issue=6284|year=1990|pages=540–544|issn=0028-0836|doi=10.1038/346540a0|pmid=2165568}}</ref> however several groups later demonstrated that this activity did not co-fractionate with RRBP1 <ref name="NunnariZimmerman1991">{{cite journal|last1=Nunnari|first1=Jodi M.|last2=Zimmerman|first2=Deborah L.|last3=Ogg|first3=Stephen C.|last4=Walter|first4=Peter|title=Characterization of the rough endoplasmic reticulum ribosome-binding activity|journal=Nature|volume=352|issue=6336|year=1991|pages=638–640|issn=0028-0836|doi=10.1038/352638a0|pmid=1650916}}</ref> | | summary_text = RRBP1 is a membrane-bound protein found in the [[endoplasmic reticulum]] (ER). It was originally identified as the ribosome receptor for the ER,<ref name="SavitzMeyer1990">{{cite journal|last1=Savitz|first1=Adam J.|last2=Meyer|first2=David I.|title=Identification of a ribosome receptor in the rough endoplasmic reticulum|journal=Nature|volume=346|issue=6284|year=1990|pages=540–544|issn=0028-0836|doi=10.1038/346540a0|pmid=2165568}}</ref> however several groups later demonstrated that this activity did not co-fractionate with RRBP1 <ref name="NunnariZimmerman1991">{{cite journal|last1=Nunnari|first1=Jodi M.|last2=Zimmerman|first2=Deborah L.|last3=Ogg|first3=Stephen C.|last4=Walter|first4=Peter|title=Characterization of the rough endoplasmic reticulum ribosome-binding activity|journal=Nature|volume=352|issue=6336|year=1991|pages=638–640|issn=0028-0836|doi=10.1038/352638a0|pmid=1650916}}</ref> | ||
<ref name="CollinsGilmore1991">{{cite journal|last1=Collins|first1=PG|last2=Gilmore|first2=R L|title=Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activity|journal=JCB|volume=114|issue=4|year=1991|pages=639–49|issn=|doi=10.1083/jcb.114.4.639}}</ref> but rather with [[Sec61]] (i.e. the [[translocon]]).<ref name="GörlichPrehn1992">{{cite journal|last1=Görlich|first1=Dirk|last2=Prehn|first2=Siegfried|last3=Hartmann|first3=Enno|last4=Kalies|first4=Kai-Uwe|last5=Rapoport|first5=Tom A.|title=A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation|journal=Cell|volume=71|issue=3|year=1992|pages=489–503|issn=0092-8674|doi=10.1016/0092-8674(92)90517-G|pmid=1423609}}</ref><ref name="Gorlich1993">{{cite journal|last1=Gorlich|first1=D|title=Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane|journal=Cell|volume=75|issue=4|year=1993|pages=615–630|issn=0092-8674|doi=10.1016/0092-8674(93)90483-7|pmid=8242738}}</ref> RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone<ref name="Cui2012">{{cite journal|last1=Cui|first1=Xianying A.|last2=Zhang|first2=Hui|last3=Palazzo|first3=Alexander F.|title=p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum|journal=PLoS Biology|volume=10|issue=5|year=2012|pages=e1001336|issn=1545-7885|doi=10.1371/journal.pbio.1001336|pmid=22679391|pmc=3362647}}</ref>}}. In addition, RRBP1 may promote the association of polysomes with the translocon <ref name="DejgaardTheberge2010">{{cite journal|last1=Dejgaard|first1=Kurt|last2=Theberge|first2=Jean-Francois|last3=Heath-Engel|first3=Hannah|last4=Chevet|first4=Eric|last5=Tremblay|first5=Michel L.|last6=Thomas|first6=David Y.|title=Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis|journal=Journal of Proteome Research|volume=9|issue=4|year=2010|pages=1763–1771|issn=1535-3893|doi=10.1021/pr900900x|pmid=20112977}}</ref><ref name="UenoKaneko2011">{{cite journal|last1=Ueno|first1=T.|last2=Kaneko|first2=K.|last3=Sata|first3=T.|last4=Hattori|first4=S.|last5=Ogawa-Goto|first5=K.|title=Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180|journal=Nucleic Acids Research|volume=40|issue=7|year=2011|pages=3006–3017|issn=0305-1048|doi=10.1093/nar/gkr1197|pmid=22156060|pmc=3326322}}</ref> and play a role in ER morphology.<ref name="ShibataShemesh2010">{{cite journal|last1=Shibata|first1=Yoko|last2=Shemesh|first2=Tom|last3=Prinz|first3=William A.|last4=Palazzo|first4=Alexander F.|last5=Kozlov|first5=Michael M.|last6=Rapoport|first6=Tom A.|title=Mechanisms Determining the Morphology of the Peripheral ER|journal=Cell|volume=143|issue=5|year=2010|pages=774–788|issn=0092-8674|doi=10.1016/j.cell.2010.11.007}}</ref> RRBP1 may also bind to [[microtubules]].<ref name="Ogawa-GotoUeno2007">{{cite journal |vauthors=Ogawa-Goto K, Tanaka K, Ueno T, etal |title=p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain |journal=Mol. Biol. Cell |volume=18 |issue= 10 |pages= 3741–51 |year= 2007 |pmid= 17634287 |doi= 10.1091/mbc.E06-12-1125 | pmc=1995732 }}</ref> Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.<ref name="entrez" /> | <ref name="CollinsGilmore1991">{{cite journal|last1=Collins|first1=PG|last2=Gilmore|first2=R L|title=Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activity|journal=JCB|volume=114|issue=4|year=1991|pages=639–49|issn=|doi=10.1083/jcb.114.4.639|citeseerx=10.1.1.282.646}}</ref> but rather with [[Sec61]] (i.e. the [[translocon]]).<ref name="GörlichPrehn1992">{{cite journal|last1=Görlich|first1=Dirk|last2=Prehn|first2=Siegfried|last3=Hartmann|first3=Enno|last4=Kalies|first4=Kai-Uwe|last5=Rapoport|first5=Tom A.|title=A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation|journal=Cell|volume=71|issue=3|year=1992|pages=489–503|issn=0092-8674|doi=10.1016/0092-8674(92)90517-G|pmid=1423609}}</ref><ref name="Gorlich1993">{{cite journal|last1=Gorlich|first1=D|title=Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane|journal=Cell|volume=75|issue=4|year=1993|pages=615–630|issn=0092-8674|doi=10.1016/0092-8674(93)90483-7|pmid=8242738}}</ref> RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone<ref name="Cui2012">{{cite journal|last1=Cui|first1=Xianying A.|last2=Zhang|first2=Hui|last3=Palazzo|first3=Alexander F.|title=p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum|journal=PLoS Biology|volume=10|issue=5|year=2012|pages=e1001336|issn=1545-7885|doi=10.1371/journal.pbio.1001336|pmid=22679391|pmc=3362647}}</ref>}}. In addition, RRBP1 may promote the association of polysomes with the translocon <ref name="DejgaardTheberge2010">{{cite journal|last1=Dejgaard|first1=Kurt|last2=Theberge|first2=Jean-Francois|last3=Heath-Engel|first3=Hannah|last4=Chevet|first4=Eric|last5=Tremblay|first5=Michel L.|last6=Thomas|first6=David Y.|title=Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis|journal=Journal of Proteome Research|volume=9|issue=4|year=2010|pages=1763–1771|issn=1535-3893|doi=10.1021/pr900900x|pmid=20112977}}</ref><ref name="UenoKaneko2011">{{cite journal|last1=Ueno|first1=T.|last2=Kaneko|first2=K.|last3=Sata|first3=T.|last4=Hattori|first4=S.|last5=Ogawa-Goto|first5=K.|title=Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180|journal=Nucleic Acids Research|volume=40|issue=7|year=2011|pages=3006–3017|issn=0305-1048|doi=10.1093/nar/gkr1197|pmid=22156060|pmc=3326322}}</ref> and play a role in ER morphology.<ref name="ShibataShemesh2010">{{cite journal|last1=Shibata|first1=Yoko|last2=Shemesh|first2=Tom|last3=Prinz|first3=William A.|last4=Palazzo|first4=Alexander F.|last5=Kozlov|first5=Michael M.|last6=Rapoport|first6=Tom A.|title=Mechanisms Determining the Morphology of the Peripheral ER|journal=Cell|volume=143|issue=5|year=2010|pages=774–788|issn=0092-8674|doi=10.1016/j.cell.2010.11.007}}</ref> RRBP1 may also bind to [[microtubules]].<ref name="Ogawa-GotoUeno2007">{{cite journal |vauthors=Ogawa-Goto K, Tanaka K, Ueno T, etal |title=p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain |journal=Mol. Biol. Cell |volume=18 |issue= 10 |pages= 3741–51 |year= 2007 |pmid= 17634287 |doi= 10.1091/mbc.E06-12-1125 | pmc=1995732 }}</ref> Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.<ref name="entrez" /> | ||
==References== | ==References== | ||
Latest revision as of 07:19, 10 January 2019
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| External IDs | GeneCards: [1] | ||||||
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| Location (UCSC) | n/a | n/a | |||||
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Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1 gene.[1][2]
RRBP1 is a membrane-bound protein found in the endoplasmic reticulum (ER). It was originally identified as the ribosome receptor for the ER,[3] however several groups later demonstrated that this activity did not co-fractionate with RRBP1 [4] [5] but rather with Sec61 (i.e. the translocon).[6][7] RRBP1 can enhance the association of certain mRNAs to the endoplasmic reticulum in a manner that does not require ribosome activity, likely by directly associating the mRNA's phosphate backbone[8]. In addition, RRBP1 may promote the association of polysomes with the translocon [9][10] and play a role in ER morphology.[11] RRBP1 may also bind to microtubules.[12] Although the p180 isoform is the most abundant, it may exist in different forms due to removal of tandem repeats by partial intraexonic splicing. RRBP1 has been excluded as a candidate gene in the cause of Alagille syndrome.[2]
References
- ↑ Basson CT, MacRae CA, Schoenberg-Fejzo M, Morton CC, Spinner NB, Genin A, Krug E, Seidman JG, Seidman CE (Dec 1996). "Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130". Genomics. 35 (3): 628–31. doi:10.1006/geno.1996.0413. PMID 8812507.
- ↑ 2.0 2.1 "Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)".
- ↑ Savitz, Adam J.; Meyer, David I. (1990). "Identification of a ribosome receptor in the rough endoplasmic reticulum". Nature. 346 (6284): 540–544. doi:10.1038/346540a0. ISSN 0028-0836. PMID 2165568.
- ↑ Nunnari, Jodi M.; Zimmerman, Deborah L.; Ogg, Stephen C.; Walter, Peter (1991). "Characterization of the rough endoplasmic reticulum ribosome-binding activity". Nature. 352 (6336): 638–640. doi:10.1038/352638a0. ISSN 0028-0836. PMID 1650916.
- ↑ Collins, PG; Gilmore, R L (1991). "Ribosome binding to the endoplasmic reticulum: a 180-kD protein identified by crosslinking to membrane-bound ribosomes is not required for ribosome binding activity". JCB. 114 (4): 639–49. CiteSeerX 10.1.1.282.646. doi:10.1083/jcb.114.4.639.
- ↑ Görlich, Dirk; Prehn, Siegfried; Hartmann, Enno; Kalies, Kai-Uwe; Rapoport, Tom A. (1992). "A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation". Cell. 71 (3): 489–503. doi:10.1016/0092-8674(92)90517-G. ISSN 0092-8674. PMID 1423609.
- ↑ Gorlich, D (1993). "Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane". Cell. 75 (4): 615–630. doi:10.1016/0092-8674(93)90483-7. ISSN 0092-8674. PMID 8242738.
- ↑ Cui, Xianying A.; Zhang, Hui; Palazzo, Alexander F. (2012). "p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum". PLoS Biology. 10 (5): e1001336. doi:10.1371/journal.pbio.1001336. ISSN 1545-7885. PMC 3362647. PMID 22679391.
- ↑ Dejgaard, Kurt; Theberge, Jean-Francois; Heath-Engel, Hannah; Chevet, Eric; Tremblay, Michel L.; Thomas, David Y. (2010). "Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis". Journal of Proteome Research. 9 (4): 1763–1771. doi:10.1021/pr900900x. ISSN 1535-3893. PMID 20112977.
- ↑ Ueno, T.; Kaneko, K.; Sata, T.; Hattori, S.; Ogawa-Goto, K. (2011). "Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180". Nucleic Acids Research. 40 (7): 3006–3017. doi:10.1093/nar/gkr1197. ISSN 0305-1048. PMC 3326322. PMID 22156060.
- ↑ Shibata, Yoko; Shemesh, Tom; Prinz, William A.; Palazzo, Alexander F.; Kozlov, Michael M.; Rapoport, Tom A. (2010). "Mechanisms Determining the Morphology of the Peripheral ER". Cell. 143 (5): 774–788. doi:10.1016/j.cell.2010.11.007. ISSN 0092-8674.
- ↑ Ogawa-Goto K, Tanaka K, Ueno T, et al. (2007). "p180 Is Involved in the Interaction between the Endoplasmic Reticulum and Microtubules through a Novel Microtubule-binding and Bundling Domain". Mol. Biol. Cell. 18 (10): 3741–51. doi:10.1091/mbc.E06-12-1125. PMC 1995732. PMID 17634287.
Further reading
- Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
- Savitz AJ, Meyer DI (1990). "Identification of a ribosome receptor in the rough endoplasmic reticulum". Nature. 346 (6284): 540–4. doi:10.1038/346540a0. PMID 2165568.
- Langley R, Leung E, Morris C, et al. (1998). "Identification of multiple forms of 180-kDa ribosome receptor in human cells". DNA Cell Biol. 17 (5): 449–60. doi:10.1089/dna.1998.17.449. PMID 9628588.
- Nagase T, Kikuno R, Ishikawa KI, et al. (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
- Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (2004). "The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B". Biochem. Biophys. Res. Commun. 319 (3): 987–92. doi:10.1016/j.bbrc.2004.05.069. PMID 15184079.
- Colland F, Jacq X, Trouplin V, et al. (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
- Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
- Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.