Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1gene.[3][4]
RRBP1 is a membrane-bound protein found in the endoplasmic reticulum (ER). It was originally identified as the ribosome receptor for the ER,[5] however several groups later demonstrated that this activity did not co-fractionate with RRBP1 [6][7] but rather with Sec61 (i.e. the translocon).[8][9] 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.[10] In addition, RRBP1 may promote the association of polysomes with the translocon [11][12] and play a role in ER morphology.[13] RRBP1 may also bind to microtubules.[14] 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.[4]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^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. PMID8812507.
^Savitz, Adam J.; Meyer, David I. (1990). "Identification of a ribosome receptor in the rough endoplasmic reticulum". Nature. 346 (6284): 540–544. Bibcode:1990Natur.346..540S. doi:10.1038/346540a0. ISSN0028-0836. PMID2165568. S2CID4353593.
^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. Bibcode:1991Natur.352..638N. doi:10.1038/352638a0. ISSN0028-0836. PMID1650916. S2CID4364699.
^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. ISSN0092-8674. PMID1423609. S2CID19078317.
^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. ISSN1535-3893. PMID20112977.
Savitz AJ, Meyer DI (1990). "Identification of a ribosome receptor in the rough endoplasmic reticulum". Nature. 346 (6284): 540–4. Bibcode:1990Natur.346..540S. doi:10.1038/346540a0. PMID2165568. S2CID4353593.
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. PMID9628588.
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. PMID15184079.
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. PMID16964243. S2CID14294292.