Biology:RRBP1

From HandWiki
Revision as of 12:19, 28 June 2023 by Ohm (talk | contribs) (over-write)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

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

  1. "Identification, characterization, and chromosomal localization of the human homolog (hES) of ES/130". Genomics 35 (3): 628–31. Dec 1996. doi:10.1006/geno.1996.0413. PMID 8812507. 
  2. 2.0 2.1 "Entrez Gene: RRBP1 ribosome binding protein 1 homolog 180kDa (dog)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6238. 
  3. 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. Bibcode1990Natur.346..540S. 
  4. 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. Bibcode1991Natur.352..638N. 
  5. 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. doi:10.1083/jcb.114.4.639. PMID 1869584. 
  6. 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. 
  7. 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. http://edoc.mdc-berlin.de/1126/1/1126oa.pdf. 
  8. 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. PMID 22679391. 
  9. 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. 
  10. 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. PMID 22156060. 
  11. 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. PMID 21111237. 
  12. "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. doi:10.1091/mbc.E06-12-1125. PMID 17634287. 

Further reading