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S100A11

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S100A11
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesS100A11, HEL-S-43, MLN70, S100C, S100 calcium binding protein A11
External IDsOMIM: 603114; MGI: 3645720; HomoloGene: 55916; GeneCards: S100A11; OMA:S100A11 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

6282

277089

Ensembl

ENSG00000163191

ENSMUSG00000066457

UniProt

P31949

n/a

RefSeq (mRNA)

NM_005620

n/a

RefSeq (protein)

NP_005611

n/a

Location (UCSC)Chr 1: 152.03 – 152.05 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene.[4][5]

Function

The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A11, also known as calgizzarin or 100C, is a small acidic protein. Along with all 13 members of the S100 family, are located as a cluster on chromosome 1q21.[6] It was first found in 1989, and later isolated from chicken gizzard muscles.[7]

The protein may function in motility, invasion, and tubulin polymerization. Chromosomal rearrangements and altered expression of this gene have been implicated in tumor metastasis.[5]

Its high expression has been found in many tissues including lung, pancreas, heart, placenta, kidney, and low levels in skeletal muscle, liver, and brain tissue.[8]

S100A11 is implicated in membrane and cytoskeletar dynamics, vesicular transportation and processes of endo and exocytosis. It has been shown that S100A11 interacts with many cytoskeletal structures as tubulin, actin, intermediate filaments also with annexin I and annexin II.[9][10] S100A11 is able to control reorganization of actin and it is important in forming protrusion by metastatic cells.[11]

It lacks enzymatic activity, it functions by binding to other proteins, it regulates activity of other enzymes.[12] It is associated with cell cycle, growth, survival and apoptosis. It has been identified as dual growth mediator.[13][6] Suppression of S100A11 by small interfering RNA caused cells to apoptosis, and overexpression of S100A11 has been found to inhibit apoptosis in tumor cells.[6] Furthermore, the knock-down of S100A11 via siRNA reduces the sister-chromatid exchange and the viability of cells.

S100A11 in pathologies

IL-8 and TNF-alpha induce the expression and release of S100A11 in chondrocytes in culture and exogenous S100A11 causes chondrocyte hypertrophy.[14] S100A11 could play a role in maintaining low-grade inflammation in osteoarthritis and in its progression.[15]

Its cellular localization is associated with the regulation of cell growth and proliferation. This protein is normally found strictly in the nucleus, but appears in the cytoplasm in cancer cells. S100A11 was localized in the cytoplasm of resting human keratinocytes in vitro.[9]

It has been shown to interact with the RAGE receptor, which is also a receptor for other S100 proteins.[14]

It is associated with low or high production in many different types of cancers. Its overproduction has been found, for example, in breast, pancreas or colectal carcinoma and its levels can be used as clinical marker in these diseases.[7]

It has been shown that S100A11 enhances the recombination activity of human RAD51 in vitro. A knock-down leads to diffuse distribution of RAD54B.[16] These finding suggest a potential role of S100A11 in the process of homologous recombination repair of double-strand breaks.[17]

Usually, S100A11 makes homodimeres, but it has been shown  that S100A11 heterodimerizes with S100B[18] and it also interacts with Nucleolin,[19] and RAD54B.[16]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163191 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Wicki R, Marenholz I, Mischke D, Schäfer BW, Heizmann CW (December 1996). "Characterization of the human S100A12 (calgranulin C, p6, CAAF1, CGRP) gene, a new member of the S100 gene cluster on chromosome 1q21". Cell Calcium. 20 (6): 459–64. doi:10.1016/S0143-4160(96)90087-1. PMID 8985590.
  5. ^ a b "Entrez Gene: S100A11 S100 calcium binding protein A11".
  6. ^ a b c Kanamori T, Takakura K, Mandai M, Kariya M, Fukuhara K, Sakaguchi M, et al. (October 2004). "Increased expression of calcium-binding protein S100 in human uterine smooth muscle tumours". Molecular Human Reproduction. 10 (10): 735–42. doi:10.1093/molehr/gah100. PMID 15322223.
  7. ^ a b Sakaguchi M, Sonegawa H, Murata H, Kitazoe M, Futami J, Kataoka K, et al. (January 2008). "S100A11, an dual mediator for growth regulation of human keratinocytes". Molecular Biology of the Cell. 19 (1): 78–85. doi:10.1091/mbc.e07-07-0682. PMC 2174196. PMID 17978094.
  8. ^ Inada H, Naka M, Tanaka T, Davey GE, Heizmann CW (September 1999). "Human S100A11 exhibits differential steady-state RNA levels in various tissues and a distinct subcellular localization". Biochemical and Biophysical Research Communications. 263 (1): 135–8. doi:10.1006/bbrc.1999.1319. PMID 10486266.
  9. ^ a b Sakaguchi M, Huh NH (October 2011). "S100A11, a dual growth regulator of epidermal keratinocytes". Amino Acids. 41 (4): 797–807. doi:10.1007/s00726-010-0747-4. PMID 20872027. S2CID 32724389.
  10. ^ Réty S, Osterloh D, Arié JP, Tabaries S, Seeman J, Russo-Marie F, et al. (February 2000). "Structural basis of the Ca(2+)-dependent association between S100C (S100A11) and its target, the N-terminal part of annexin I". Structure. 8 (2): 175–84. doi:10.1016/s0969-2126(00)00093-9. PMID 10673436.
  11. ^ Shankar J, Messenberg A, Chan J, Underhill TM, Foster LJ, Nabi IR (May 2010). "Pseudopodial actin dynamics control epithelial-mesenchymal transition in metastatic cancer cells". Cancer Research. 70 (9): 3780–90. doi:10.1158/0008-5472.can-09-4439. PMID 20388789.
  12. ^ Zhao XQ, Naka M, Muneyuki M, Tanaka T (January 2000). "Ca(2+)-dependent inhibition of actin-activated myosin ATPase activity by S100C (S100A11), a novel member of the S100 protein family". Biochemical and Biophysical Research Communications. 267 (1): 77–9. doi:10.1006/bbrc.1999.1918. PMID 10623577.
  13. ^ He H, Li J, Weng S, Li M, Yu Y (2009). "S100A11: diverse function and pathology corresponding to different target proteins". Cell Biochemistry and Biophysics. 55 (3): 117–26. doi:10.1007/s12013-009-9061-8. PMID 19649745. S2CID 19509620.
  14. ^ a b Cecil DL, Johnson K, Rediske J, Lotz M, Schmidt AM, Terkeltaub R (December 2005). "Inflammation-induced chondrocyte hypertrophy is driven by receptor for advanced glycation end products". Journal of Immunology. 175 (12): 8296–302. doi:10.4049/jimmunol.175.12.8296. PMID 16339570.
  15. ^ Cecil DL, Terkeltaub R (June 2008). "Transamidation by transglutaminase 2 transforms S100A11 calgranulin into a procatabolic cytokine for chondrocytes". Journal of Immunology. 180 (12): 8378–85. doi:10.4049/jimmunol.180.12.8378. PMC 2577366. PMID 18523305.
  16. ^ a b Murzik U, Hemmerich P, Weidtkamp-Peters S, Ulbricht T, Bussen W, Hentschel J, et al. (July 2008). "Rad54B targeting to DNA double-strand break repair sites requires complex formation with S100A11". Molecular Biology of the Cell. 19 (7): 2926–35. doi:10.1091/mbc.e07-11-1167. PMC 2441681. PMID 18463164.
  17. ^ Foertsch F, Szambowska A, Weise A, Zielinski A, Schlott B, Kraft F, et al. (October 2016). "S100A11 plays a role in homologous recombination and genome maintenance by influencing the persistence of RAD51 in DNA repair foci". Cell Cycle. 15 (20): 2766–79. doi:10.1080/15384101.2016.1220457. PMC 5053559. PMID 27590262.
  18. ^ Deloulme JC, Assard N, Mbele GO, Mangin C, Kuwano R, Baudier J (November 2000). "S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo". The Journal of Biological Chemistry. 275 (45): 35302–10. doi:10.1074/jbc.M003943200. PMID 10913138.
  19. ^ Sakaguchi M, Miyazaki M, Takaishi M, Sakaguchi Y, Makino E, Kataoka N, et al. (November 2003). "S100C/A11 is a key mediator of Ca(2+)-induced growth inhibition of human epidermal keratinocytes". The Journal of Cell Biology. 163 (4): 825–35. doi:10.1083/jcb.200304017. PMC 2173690. PMID 14623863.

Further reading

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