Thymopoietin

(Redirected from TMPO)

Lamina-associated polypeptide 2 (LAP2), isoforms beta/gamma is a protein that in humans is encoded by the TMPO gene.[5][6] LAP2 is an inner nuclear membrane (INM) protein.[7]

TMPO
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesTMPO, CMD1T, LAP2, LEMD4, PRO0868, TP, thymopoietin
External IDsOMIM: 188380; MGI: 106920; HomoloGene: 31144; GeneCards: TMPO; OMA:TMPO - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001032283
NM_001032284
NM_001307975
NM_003276

RefSeq (protein)
Location (UCSC)Chr 12: 98.52 – 98.55 MbChr 10: 90.98 – 91.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Thymopoietin is a protein involved in the induction of CD90 in the thymus. The thymopoetin (TMPO) gene encodes three alternatively spliced mRNAs encoding proteins of 75 kDa (alpha), 51 kDa (beta) and 39 kDa (gamma) which are ubiquitously expressed in all cells. The human TMPO gene maps to chromosome band 12q22 and consists of eight exons. TMPO alpha is present diffusely expressed with the cell nucleus while TMPO beta and gamma are localized to the nuclear membrane. TMPO beta is a human homolog of the murine protein LAP2. LAP2 plays a role in the regulation of nuclear architecture by binding lamin B1 and chromosomes. This interaction is regulated by phosphorylation during mitosis. Given the nuclear localization of the three TMPO isoforms, it is unlikely that these proteins play any role in CD90 induction.

Interactions

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Thymopoietin has been shown to interact with Barrier to autointegration factor 1,[8] AKAP8L,[9][10] LMNB1[11][12] and LMNA.[13][14]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000120802Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000019961Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Harris CA, Andryuk PJ, Cline S, Chan HK, Natarajan A, Siekierka JJ, Goldstein G (Jul 1994). "Three distinct human thymopoietins are derived from alternatively spliced mRNAs". Proceedings of the National Academy of Sciences of the United States of America. 91 (14): 6283–7. Bibcode:1994PNAS...91.6283H. doi:10.1073/pnas.91.14.6283. PMC 44185. PMID 7517549.
  6. ^ "Entrez Gene: TMPO thymopoietin".
  7. ^ Holmer L, Worman HJ (Nov 2001). "Inner nuclear membrane proteins: functions and targeting". Cellular and Molecular Life Sciences. 58 (12–13): 1741–7. doi:10.1007/PL00000813. PMC 11337314. PMID 11766875. S2CID 20902309.
  8. ^ Furukawa K (Aug 1999). "LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction". Journal of Cell Science. 112 ( Pt 15) (15): 2485–92. doi:10.1242/jcs.112.15.2485. PMID 10393804.
  9. ^ Martins SB, Eide T, Steen RL, Jahnsen T, Skålhegg BS, Collas P (Nov 2000). "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics". Journal of Cell Science. 113 Pt 21 (21): 3703–13. doi:10.1242/jcs.113.21.3703. PMID 11034899.
  10. ^ Martins S, Eikvar S, Furukawa K, Collas P (Jan 2003). "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication". The Journal of Cell Biology. 160 (2): 177–88. doi:10.1083/jcb.200210026. PMC 2172640. PMID 12538639.
  11. ^ Furukawa K, Kondo T (Feb 1998). "Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin". European Journal of Biochemistry. 251 (3): 729–33. doi:10.1046/j.1432-1327.1998.2510729.x. PMID 9490046.
  12. ^ Foisner R, Gerace L (Jul 1993). "Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation". Cell. 73 (7): 1267–79. doi:10.1016/0092-8674(93)90355-T. PMID 8324822. S2CID 10641633.
  13. ^ Markiewicz E, Dechat T, Foisner R, Quinlan RA, Hutchison CJ (Dec 2002). "Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein". Molecular Biology of the Cell. 13 (12): 4401–13. doi:10.1091/mbc.E02-07-0450. PMC 138642. PMID 12475961.
  14. ^ Dechat T, Korbei B, Vaughan OA, Vlcek S, Hutchison CJ, Foisner R (Oct 2000). "Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins". Journal of Cell Science. 113 Pt 19 (19): 3473–84. doi:10.1242/jcs.113.19.3473. PMID 10984438.

Further reading

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