RRBP1 explained

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.

Further reading

• Nakajima D, Okazaki N, Yamakawa H, etal . Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones . DNA Res. . 9 . 3 . 99–106 . 2003 . 12168954 . 10.1093/dnares/9.3.99 . free .
• Savitz AJ, Meyer DI . Identification of a ribosome receptor in the rough endoplasmic reticulum . Nature . 346 . 6284 . 540–4 . 1990 . 2165568 . 10.1038/346540a0 . 1990Natur.346..540S . 4353593 .
• Langley R, Leung E, Morris C, etal . Identification of multiple forms of 180-kDa ribosome receptor in human cells . DNA Cell Biol. . 17 . 5 . 449–60 . 1998 . 9628588 . 10.1089/dna.1998.17.449 .
• Nagase T, Kikuno R, Ishikawa KI, etal . 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 . 2000 . 10718198 . 10.1093/dnares/7.1.65 . free .
• Deloukas P, Matthews LH, Ashurst J, etal . The DNA sequence and comparative analysis of human chromosome 20 . Nature . 414 . 6866 . 865–71 . 2002 . 11780052 . 10.1038/414865a . 2001Natur.414..865D . free .
• Strausberg RL, Feingold EA, Grouse LH, etal . 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 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL . The ribosome receptor, p180, interacts with kinesin heavy chain, KIF5B . Biochem. Biophys. Res. Commun. . 319 . 3 . 987–92 . 2004 . 15184079 . 10.1016/j.bbrc.2004.05.069 .
• Colland F, Jacq X, Trouplin V, etal . Functional Proteomics Mapping of a Human Signaling Pathway . Genome Res. . 14 . 7 . 1324–32 . 2004 . 15231748 . 10.1101/gr.2334104 . 442148 .
• Beausoleil SA, Jedrychowski M, Schwartz D, etal . Large-scale characterization of HeLa cell nuclear phosphoproteins . Proc. Natl. Acad. Sci. U.S.A. . 101 . 33 . 12130–5 . 2004 . 15302935 . 10.1073/pnas.0404720101 . 514446 . 2004PNAS..10112130B . free .
• Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Beausoleil SA, Villén J, Gerber SA, etal . A probability-based approach for high-throughput protein phosphorylation analysis and site localization . Nat. Biotechnol. . 24 . 10 . 1285–92 . 2006 . 16964243 . 10.1038/nbt1240 . 14294292 .
• Olsen JV, Blagoev B, Gnad F, etal . Global, in vivo, and site-specific phosphorylation dynamics in signaling networks . Cell . 127 . 3 . 635–48 . 2006 . 17081983 . 10.1016/j.cell.2006.09.026 . 7827573 . free .
• Ewing RM, Chu P, Elisma F, etal . Large-scale mapping of human protein–protein interactions by mass spectrometry . Mol. Syst. Biol. . 3 . 1. 89 . 2007 . 17353931 . 10.1038/msb4100134 . 1847948 .

Notes and References

1. Basson CT, MacRae CA, Schoenberg-Fejzo M, Morton CC, Spinner NB, Genin A, Krug E, Seidman JG, Seidman CE . Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130 . Genomics . 35 . 3 . 628–31 . Dec 1996 . 8812507 . 10.1006/geno.1996.0413 . free .
2. Web site: Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog).
3. Savitz. Adam J.. Meyer. David I.. Identification of a ribosome receptor in the rough endoplasmic reticulum. Nature. 346. 6284. 1990. 540–544. 0028-0836. 10.1038/346540a0. 2165568. 1990Natur.346..540S. 4353593.
4. Nunnari. Jodi M.. Zimmerman. Deborah L.. Ogg. Stephen C.. Walter. Peter. Characterization of the rough endoplasmic reticulum ribosome-binding activity. Nature. 352. 6336. 1991. 638–640. 0028-0836. 10.1038/352638a0. 1650916. 1991Natur.352..638N. 4364699.
5. Collins. PG. Gilmore. R L. 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 of Cell Biology. 114. 4. 1991. 639–49. 10.1083/jcb.114.4.639. 1869584. 2289890. 10.1.1.282.646.
6. Görlich. Dirk. Prehn. Siegfried. Hartmann. Enno. Kalies. Kai-Uwe. Rapoport. Tom A.. A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell. 71. 3. 1992. 489–503. 0092-8674. 10.1016/0092-8674(92)90517-G. 1423609. 19078317.
7. Gorlich. D. Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell. 75. 4. 1993. 615–630. 0092-8674. 10.1016/0092-8674(93)90483-7. 8242738. 5476342. free.
8. Cui. Xianying A.. Zhang. Hui. Palazzo. Alexander F.. p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum. PLOS Biology. 10. 5. 2012. e1001336. 1545-7885. 10.1371/journal.pbio.1001336. 22679391. 3362647 . free .
9. Dejgaard. Kurt. Theberge. Jean-Francois. Heath-Engel. Hannah. Chevet. Eric. Tremblay. Michel L.. Thomas. David Y.. Organization of the Sec61 Translocon, Studied by High Resolution Native Electrophoresis. Journal of Proteome Research. 9. 4. 2010. 1763–1771. 1535-3893. 10.1021/pr900900x. 20112977.
10. Ueno. T.. Kaneko. K.. Sata. T.. Hattori. S.. Ogawa-Goto. K.. Regulation of polysome assembly on the endoplasmic reticulum by a coiled-coil protein, p180. Nucleic Acids Research. 40. 7. 2011. 3006–3017. 0305-1048. 10.1093/nar/gkr1197. 22156060. 3326322.
11. Shibata. Yoko. Shemesh. Tom. Prinz. William A.. Palazzo. Alexander F.. Kozlov. Michael M.. Rapoport. Tom A.. Mechanisms Determining the Morphology of the Peripheral ER. Cell. 143. 5. 2010. 774–788. 0092-8674. 10.1016/j.cell.2010.11.007. 21111237. 3008339.
12. Ogawa-Goto K, Tanaka K, Ueno T, etal . 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 . 2007 . 17634287 . 10.1091/mbc.E06-12-1125 . 1995732 .