BYSL

BYSL
Identifiers
Aliases	BYSL, BYSTIN, bystin like
External IDs	MGI: 1858419 HomoloGene: 2991 GeneCards: BYSL
Gene ontology Molecular function • protein binding • poly(A) RNA binding Cellular component • cytoplasm • membrane • intracellular membrane-bounded organelle • apical part of cell • nucleolus • nucleus • cytosol • nucleoplasm Biological process • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) • ribosome biogenesis • female pregnancy • in utero embryonic development • blastocyst formation • cell adhesion • trophectodermal cell differentiation • cell proliferation • rRNA processing Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	705	53414
Ensembl	ENSG00000112578	ENSMUSG00000023988
UniProt	Q13895	O54825
RefSeq (mRNA)	NM_004053	NM_016859
RefSeq (protein)	NP_004044.3	NP_058555.3
Location (UCSC)	Chr 6: 41.92 – 41.93 Mb	Chr 17: 47.6 – 47.61 Mb
PubMed search	[1]	[2]
Wikidata

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Bystin is a protein that in humans is encoded by the BYSL gene.^[3][4][5]

Function

Bystin is expressed as a 2-kb major transcript and a 3.6-kb minor transcript in SNG-M cells and in human trophoblastic teratocarcinoma HT-H cells. Protein binding assays determined that bystin binds directly to trophinin and tastin, and that binding is enhanced when cytokeratins 8 and 18 are present. Immunocytochemistry of HT-H cells showed that bystin colocalizes with trophinin, tastin, and the cytokeratins, suggesting that these molecules form a complex in trophectoderm cells at the time of implantation. Using immunohistochemistry it was determined that trophinin and bystin are found in the placenta from the sixth week of pregnancy. Both proteins were localized in the cytoplasm of the syncytiotrophoblast in the chorionic villi and in endometrial decidual cells at the uteroplacental interface. After week 10, the levels of trophinin, tastin, and bystin decreased and then disappeared from placental villi.^[5]

Interactions

BYSL has been shown to interact with TROAP.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Pack SD, Pak E, Tanigami A, Ledbetter DH, Fukuda MN (Mar 1999). "Assignment1 of the bystin gene BYSL to human chromosome band 6p21.1 by in situ hybridization". Cytogenet Cell Genet. 83 (1–2): 76–7. doi:10.1159/000015131. PMID 9925933.
4. Miyoshi M, Okajima T, Matsuda T, Fukuda MN, Nadano D (May 2007). "Bystin in human cancer cells: intracellular localization and function in ribosome biogenesis". Biochem J. 404 (3): 373–81. doi:10.1042/BJ20061597. PMC 1896285. PMID 17381424.
5. "Entrez Gene: BYSL bystin-like".
6. Suzuki N, Zara J, Sato T, Ong E, Bakhiet N, Oshima RG, Watson KL, Fukuda MN (Apr 1998). "A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells". Proc. Natl. Acad. Sci. U.S.A. 95 (9): 5027–32. doi:10.1073/pnas.95.9.5027. PMC 20207. PMID 9560222.

Further reading

• Suzuki N, Zara J, Sato T, Ong E, Bakhiet N, Oshima RG, Watson KL, Fukuda MN (1998). "A cytoplasmic protein, bystin, interacts with trophinin, tastin, and cytokeratin and may be involved in trophinin-mediated cell adhesion between trophoblast and endometrial epithelial cells.". Proc. Natl. Acad. Sci. U.S.A. 95 (9): 5027–32. doi:10.1073/pnas.95.9.5027. PMC 20207. PMID 9560222.
• Suzuki N, Nakayama J, Shih IM, Aoki D, Nozawa S, Fukuda MN (1999). "Expression of trophinin, tastin, and bystin by trophoblast and endometrial cells in human placenta.". Biol. Reprod. 60 (3): 621–7. doi:10.1095/biolreprod60.3.621. PMID 10026108.
• Nakayama J, Aoki D, Suga T, Akama TO, Ishizone S, Yamaguchi H, Imakawa K, Nadano D, Fazleabas AT, Katsuyama T, Nozawa S, Fukuda MN (2004). "Implantation-dependent expression of trophinin by maternal fallopian tube epithelia during tubal pregnancies: possible role of human chorionic gonadotrophin on ectopic pregnancy.". Am. J. Pathol. 163 (6): 2211–9. doi:10.1016/S0002-9440(10)63579-1. PMC 1892375. PMID 14633596.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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.