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RRBP1

From Wikipedia, the free encyclopedia
RRBP1
Identifiers
AliasesRRBP1, ES/130, ES130, RRp, hES, ribosome binding protein 1, p180
External IDsOMIM: 601418; HomoloGene: 136784; GeneCards: RRBP1; OMA:RRBP1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004587
NM_001042576
NM_001365613

n/a

RefSeq (protein)

NP_001036041
NP_004578
NP_001352542

n/a

Location (UCSC)Chr 20: 17.61 – 17.68 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

Ribosome-binding protein 1, also referred to as p180, is a protein that in humans is encoded by the RRBP1 gene.[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]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125844Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ 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.
  4. ^ a b "Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)".
  5. ^ 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. ISSN 0028-0836. PMID 2165568. S2CID 4353593.
  6. ^ 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. ISSN 0028-0836. PMID 1650916. S2CID 4364699.
  7. ^ 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". Journal of Cell Biology. 114 (4): 639–49. CiteSeerX 10.1.1.282.646. doi:10.1083/jcb.114.4.639. PMC 2289890. PMID 1869584.
  8. ^ 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. S2CID 19078317.
  9. ^ Gorlich, D (1993). "Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane" (PDF). Cell. 75 (4): 615–630. doi:10.1016/0092-8674(93)90483-7. ISSN 0092-8674. PMID 8242738. S2CID 5476342.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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. PMC 3008339. PMID 21111237.
  14. ^ 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

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