View source for HSP90AB1

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{cs1 config|name-list-style=vanc}}
{{Infobox_gene}}
'''Heat shock protein HSP 90-beta''' also called '''HSP90beta''' is a [[protein]] that in humans is encoded by the ''HSP90AB1'' [[gene]].<ref name="pmid2768249">{{cite journal | vauthors = Rebbe NF, Hickman WS, Ley TJ, Stafford DW, Hickman S | title = Nucleotide sequence and regulation of a human 90-kDa heat shock protein gene | journal = The Journal of Biological Chemistry | volume = 264 | issue = 25 | pages = 15006–11 | date = Sep 1989 | doi = 10.1016/S0021-9258(18)63803-7 | pmid = 2768249 | doi-access = free }}</ref><ref name="pmid16269234">{{cite journal | vauthors = Chen B, Piel WH, Gui L, Bruford E, Monteiro A | title = The HSP90 family of genes in the human genome: insights into their divergence and evolution | journal = Genomics | volume = 86 | issue = 6 | pages = 627–37 | date = Dec 2005 | pmid = 16269234 | doi = 10.1016/j.ygeno.2005.08.012 | doi-access = free }}</ref><ref>{{cite web | title = NCBI Gene: HSP90AB1 heat shock protein 90 alpha family class B member 1| url = https://www.ncbi.nlm.nih.gov/gene/3326| access-date = 2019-08-30}}</ref>

== Function ==
HSP90AB1 is a [[molecular chaperone]]. Chaperones are proteins that bind to other proteins, thereby stabilizing them<ref>{{cite journal | vauthors = Lindquist S | title = The heat-shock response | journal = Annual Review of Biochemistry | volume = 55 | issue = 1 | pages = 1151–1191 | date = June 1986 | pmid = 2427013 | doi = 10.1146/annurev.bi.55.070186.005443 | s2cid = 42450279 }}</ref><ref>{{cite journal | vauthors = Gething MJ, Sambrook J | title = Protein folding in the cell | journal = Nature | volume = 355 | issue = 6355 | pages = 33–45 | date = Jan 1992 | pmid = 1731198 | doi = 10.1038/355033a0 | bibcode = 1992Natur.355...33G | s2cid = 4330003 }}</ref><ref>{{cite journal | vauthors = Craig EA, Gambill BD, Nelson RJ | title = Heat shock proteins: molecular chaperones of protein biogenesis | journal = Microbiological Reviews | volume = 57 | issue = 2 | pages = 402–14 | date = Jun 1993 | doi = 10.1128/MMBR.57.2.402-414.1993 | pmid = 8336673 | pmc=372916}}</ref><ref>{{cite journal | vauthors = Hartl FU | title = Molecular chaperones in cellular protein folding | journal = Nature | volume = 381 | issue = 6583 | pages = 571–9 | date = Jun 1996 | pmid = 8637592 | doi = 10.1038/381571a0 | bibcode = 1996Natur.381..571H | s2cid = 4347271 }}</ref><ref>{{cite journal | vauthors = Johnson JL, Craig EA | title = Protein folding in vivo: unraveling complex pathways | journal = Cell | volume = 90 | issue = 2 | pages = 201–4 | date = Jul 1997 | pmid = 9244293 | doi=10.1016/s0092-8674(00)80327-x| s2cid = 16824153 | doi-access = free }}</ref><ref>{{cite book | vauthors = Wegele H, Müller L, Buchner J | title = Hsp70 and Hsp90--a relay team for protein folding | journal = Reviews of Physiology, Biochemistry and Pharmacology | volume = 151 | pages = 1–44 | date = 2004 | pmid = 14740253 | doi = 10.1007/s10254-003-0021-1 | isbn = 978-3-540-22096-1 }}</ref><ref name="ReferenceA">{{cite journal | vauthors = Taipale M, Jarosz DF, Lindquist S | title = HSP90 at the hub of protein homeostasis: emerging mechanistic insights | journal = Nature Reviews Molecular Cell Biology | volume = 11 | issue = 7 | pages = 515–28 | date = Jul 2010 | pmid = 20531426 | doi = 10.1038/nrm2918 | s2cid = 7842137 }}</ref> in an [[adenosine triphosphate|ATP]]-dependent manner.<ref name="Obermann WM p90">{{cite journal | vauthors = Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU | title = In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis | journal = The Journal of Cell Biology | volume = 143 | issue = 4 | pages = 901–10 | date = Nov 1998 | pmid = 9817749 | doi=10.1083/jcb.143.4.901 | pmc=2132952}}</ref> Chaperones stabilize new proteins during translation, mature proteins which are partially unstable but also proteins that have become partially [[Denaturation (biochemistry)|denatured]] due to various kinds of cellular stress. In case proper [[protein folding|folding]] or refolding is impossible, HSPs mediate protein degradation. They also have specialized functions, such as intracellular transport into [[organelle]]s.

== Classification ==
{{main|Heat shock protein}}
Human HSPs are classified into 5 major groups according to the [[HGNC]]:<ref name="HGNC Heat Shock Protein Group">{{cite web|url=https://www.genenames.org/data/genegroup/#!/group/582|website=HUGO Gene Nomenclature Committee (HGNC)|access-date=30 August 2019|title=Gene group &#124; HUGO Gene Nomenclature Committee}}</ref><ref name="ReferenceB">{{cite journal | vauthors = Kampinga HH, Hageman J, Vos MJ, Kubota H, Tanguay RM, Bruford EA, Cheetham ME, Chen B, Hightower LE | title = Guidelines for the nomenclature of the human heat shock proteins | journal = Cell Stress & Chaperones | volume = 14 | issue = 1 | pages = 105–11 | date = Jan 2009 | pmid = 18663603 | doi = 10.1007/s12192-008-0068-7 | pmc=2673902}}</ref>
* [[HSP70]]
* [[DnaJ]] (HSP40)
* HSPB (small heat shock proteins)
* HSPC (HSP90)
* [[chaperonin]]s
Chaperonins are characterized by their barrel-shaped structure with binding sites for client proteins inside the barrels.

The human HSP90 group consists of 5 members according to the [[HGNC]]:<ref name="ReferenceB"/><ref name="HGNC HSP90 Group">{{cite web | title = HGNC HSP90 Group | url = https://www.genenames.org/data/genegroup/#!/group/586 | website = HUGO Gene Nomenclature Committee (HGNC) | access-date = 30 August 2019}}</ref>
* [[HSP90AA1]] (heat shock protein 90 kDa alpha, class A, member 1)
* HSP90AA3P (heat shock protein 90 alpha family class A member 3, pseudogene)
* HSP90AB1 (heat shock protein 90 kDa alpha, class B, member 1) (this protein)
* [[HSP90B1]] (heat shock protein 90 kDA beta, member 1)
* [[TRAP1]] (TNF receptor associated protein 1)
Whereas HSP90AA1 and HSP90AB1 are located primarily in the cytoplasm of the cells, HSP90B1 can be found in the endoplasmic reticulum and Trap1 in mitochondria.

== Co-chaperones ==
Co-chaperones bind to HSPs and influence their activity, substrate (client) specificity and interaction with other HSPs.<ref name="ReferenceA"/> For example, the co-chaperone [[CDC37]] (cell division cycle 37) stabilizes the cell cycle regulatory proteins [[CDK4]] (cyclin dependent kinase 4) and Cdk6.<ref>{{cite journal | vauthors = Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, Draetta GF, Gyuris J | title = Interaction between Cdc37 and Cdk4 in human cells | journal = Oncogene | volume = 14 | issue = 16 | pages = 1999–2004 | date = Apr 1997 | pmid = 9150368 | doi = 10.1038/sj.onc.1201036 | s2cid = 25236893 | doi-access =  }}</ref> [[Hop (protein)|Hop]] (HSP organizing protein) mediates the interaction between different HSPs, forming [[HSP70]]–[[HSP90]] complexes.<ref>{{cite journal | vauthors = Chen S, Smith DF | title = Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery | journal = The Journal of Biological Chemistry | volume = 273 | issue = 52 | pages = 35194–200 | date = Dec 1998 | pmid = 9857057 | doi=10.1074/jbc.273.52.35194| doi-access = free }}</ref><ref name="Scheufler C p70">{{cite journal | vauthors = Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I | title = Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine | journal = Cell | volume = 101 | issue = 2 | pages = 199–210 | date = Apr 2000 | pmid = 10786835 | doi = 10.1016/S0092-8674(00)80830-2 | s2cid = 18200460 | doi-access = free }}</ref> [[TOMM70A|TOM70]] (translocase of the outer mitochondrial membrane of ~70 kDa) mediates translocation of client proteins through the import pore into the [[mitochondrial matrix]].<ref name="Scheufler C p70"/><ref>{{cite journal | vauthors = Young JC, Hoogenraad NJ, Hartl FU | title = Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70 | journal = Cell | volume = 112 | issue = 1 | pages = 41–50 | date = Jan 2003 | pmid = 12526792 | doi=10.1016/s0092-8674(02)01250-3| doi-access = free }}</ref>

== Isoforms ==
Human HPS90AB1 shares 60% overall homology to its closest relative [[HSP90AA1]].<ref>{{cite journal | vauthors = Rebbe NF, Ware J, Bertina RM, Modrich P, Stafford DW | title = Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family | journal = Gene | volume = 53 | issue = 2–3 | pages = 235–45 | date = 1987 | pmid = 3301534 | doi=10.1016/0378-1119(87)90012-6}}</ref> Murine HSP90AB1 was cloned in 1987 based on homology of the corresponding ''[[Drosophila melanogaster]]'' gene.<ref>{{cite journal | vauthors = Moore SK, Kozak C, Robinson EA, Ullrich SJ, Appella E | title = Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences | journal = Gene | volume = 56 | issue = 1 | pages = 29–40 | date = 1987 | pmid = 2445630 | doi=10.1016/0378-1119(87)90155-7| url = https://zenodo.org/record/1258507 }}</ref><ref>{{cite journal | vauthors = Moore SK, Kozak C, Robinson EA, Ullrich SJ, Appella E | title = Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome assignments, and evolutionary origins | journal = The Journal of Biological Chemistry | volume = 264 | issue = 10 | pages = 5343–51 | date = Apr 1989 | doi = 10.1016/S0021-9258(18)83551-7 | pmid = 2925609 | doi-access = free }}</ref>

== Protein structure ==
HSP90AB1 is active as [[homodimer]], forming a V-shaped structure.<ref name="Scheufler C p70"/><ref>{{cite journal | vauthors = Prodromou C, Roe SM, Piper PW, Pearl LH | title = A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone | journal = Nature Structural Biology | volume = 4 | issue = 6 | pages = 477–82 | date = Jun 1997 | pmid = 9187656 | doi=10.1038/nsb0697-477| s2cid = 38764610 }}</ref><ref>{{cite journal | vauthors = Stebbins CE, Russo AA, Schneider C, Rosen N, Hartl FU, Pavletich NP | title = Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent | journal = Cell | volume = 89 | issue = 2 | pages = 239–50 | date = Apr 1997 | pmid = 9108479 | doi=10.1016/s0092-8674(00)80203-2| s2cid = 5253110 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Harris SF, Shiau AK, Agard DA | title = The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site | journal = Structure | volume = 12 | issue = 6 | pages = 1087–97 | date = Jun 2004 | pmid = 15274928 | doi = 10.1016/j.str.2004.03.020 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH | title = Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex | journal = Nature | volume = 440 | issue = 7087 | pages = 1013–7 | date = Apr 2006 | pmid = 16625188 | pmc = 5703407 | doi = 10.1038/nature04716 | bibcode = 2006Natur.440.1013A }}</ref><ref>{{cite journal | vauthors = Shiau AK, Harris SF, Southworth DR, Agard DA | title = Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements | journal = Cell | volume = 127 | issue = 2 | pages = 329–40 | date = Oct 2006 | pmid = 17055434 | doi = 10.1016/j.cell.2006.09.027 | s2cid = 406855 | doi-access = free }}</ref>
It consists of three major domains:
* [[N-terminal]] domain (NTD) containing the ATP binding site
* middle domain, primarily responsible for substrate binding
* [[C-terminal]] domain (CTD) which is the dimerization domain (base of the V).
Between these domains, there are short charged domains. Co-chaperones primarily bind to the NTD and CTD. The latter Co-chaperones usually contain a [[Tetratricopeptide|tetratricopeptide repeat]] (TPR) domain which binds to a MEEVD motif at the C-terminus of the HSP.<ref name="Scheufler C p70"/><ref>{{cite journal | vauthors = Young JC, Obermann WM, Hartl FU | title = Specific binding of tetratricopeptide repeat proteins to the C-terminal 12-kDa domain of hsp90 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 29 | pages = 18007–10 | date = Jul 1998 | pmid = 9660753 | doi=10.1074/jbc.273.29.18007| doi-access = free }}</ref> Inhibition of HSP90 activity by [[geldanamycin]] derivatives is based on their binding to the ATP binding site.<ref name="Obermann WM p90"/>

== Client proteins ==
Client proteins are [[steroid hormone receptor]]s, [[kinase]]s, [[ubiquitin ligase]]s, [[transcription factor]]s and proteins from many more families.<ref name="ReferenceA"/><ref>{{cite journal | vauthors = Tsaytler PA, Krijgsveld J, Goerdayal SS, Rüdiger S, Egmond MR | title = Novel Hsp90 partners discovered using complementary proteomic approaches | journal = Cell Stress & Chaperones | volume = 14 | issue = 6 | pages = 629–38 | date = Nov 2009 | pmid = 19396626 | doi = 10.1007/s12192-009-0115-z | pmc=2866955}}</ref><ref>{{cite journal | vauthors = Echeverría PC, Bernthaler A, Dupuis P, Mayer B, Picard D | title = An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine | journal = PLOS ONE | volume = 6 | issue = 10 | pages = e26044 | date = 2011 | pmid = 22022502 | doi = 10.1371/journal.pone.0026044 | pmc=3195953| bibcode = 2011PLoSO...626044E | doi-access = free }}</ref> Examples of HSP90AB1 client proteins are p38MAPK/[[MAPK14]] (mitogen activated protein kinase 14),<ref>{{cite journal | vauthors = Bandyopadhyay S, Chiang CY, Srivastava J, Gersten M, White S, Bell R, Kurschner C, Martin C, Smoot M, Sahasrabudhe S, Barber DL, Chanda SK, Ideker T | title = A human MAP kinase interactome | journal = Nature Methods | volume = 7 | issue = 10 | pages = 801–5 | date = Oct 2010 | pmid = 20936779 | doi=10.1038/nmeth.1506 | pmc=2967489}}</ref> [[ERK5]] (extracellular regulated kinase 5),<ref>{{cite journal | vauthors = Erazo T, Moreno A, Ruiz-Babot G, Rodríguez-Asiain A, Morrice NA, Espadamala J, Bayascas JR, Gómez N, Lizcano JM | title = Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex | journal = Molecular and Cellular Biology | volume = 33 | issue = 8 | pages = 1671–86 | date = Apr 2013 | pmid = 23428871 | doi = 10.1128/MCB.01246-12 | pmc=3624243}}</ref> or the checkpoint kinase [[Wee1]].<ref>{{cite journal | vauthors = Aressy B, Jullien D, Cazales M, Marcellin M, Bugler B, Burlet-Schiltz O, Ducommun B | title = A screen for deubiquitinating enzymes involved in the G₂/M checkpoint identifies USP50 as a regulator of HSP90-dependent Wee1 stability | journal = Cell Cycle | volume = 9 | issue = 18 | pages = 3815–22 | date = Sep 2010 | pmid = 20930503 | doi = 10.4161/cc.9.18.13133 | doi-access = free }}</ref>

== Clinical significance ==
[[Cystic fibrosis]] (CF, mucoviscidosis) is a genetic disease with increased viscosity of various secretions leading to organ failure of lung, pancreas and other organs. It is caused in nearly all cases by a deletion of phenylalanine 508 of [[cystic fibrosis transmembrane conductance regulator|CFTR]] (cystic fibrosis transmembrane conductance regulator). This mutation causes a maturation defect of this [[ion channel]] protein with increased degradation, mediated by HSPs. Deletion of the co-chaperone [[AHSA1|AHA1]] (activator of heat shock 90kDa protein ATPase homolog 1) leads to stabilization of CFTR and opens up a perspective for a new therapy.<ref>{{cite journal | vauthors = Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, Coppinger J, Gurkan C, Kellner W, Matteson J, Plutner H, Riordan JR, Kelly JW, Yates JR, Balch WE | title = Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis | journal = Cell | volume = 127 | issue = 4 | pages = 803–15 | date = Nov 2006 | pmid = 17110338 | doi = 10.1016/j.cell.2006.09.043 | s2cid = 1457851 | doi-access = free }}</ref>

=== Cancer ===
HSP90AB1 and its co-chaperones are frequently overexpressed in cancer cells.<ref>{{cite journal | vauthors = McDowell CL, Bryan Sutton R, Obermann WM | title = Expression of Hsp90 chaperone [corrected] proteins in human tumor tissue | journal = International Journal of Biological Macromolecules | volume = 45 | issue = 3 | pages = 310–4 | date = Oct 2009 | pmid = 19576239 | doi = 10.1016/j.ijbiomac.2009.06.012 }}</ref> They are able to stabilize mutant proteins thereby allowing survival and increased proliferation of cancer cells. This renders HSPs potential targets for cancer treatment.<ref>{{cite journal | vauthors = Den RB, Lu B | title = Heat shock protein 90 inhibition: rationale and clinical potential | journal = Therapeutic Advances in Medical Oncology | volume = 4 | issue = 4 | pages = 211–8 | date = Jul 2012 | pmid = 22754594 | doi = 10.1177/1758834012445574 | pmc=3384095}}</ref><ref>{{cite journal | vauthors = Jhaveri K, Taldone T, Modi S, Chiosis G | title = Advances in the clinical development of heat shock protein 90 (Hsp90) inhibitors in cancers | journal = Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | volume = 1823 | issue = 3 | pages = 742–55 | date = Mar 2012 | pmid = 22062686 | doi = 10.1016/j.bbamcr.2011.10.008 | pmc=3288123}}</ref><ref>{{cite journal | vauthors = Hong DS, Banerji U, Tavana B, George GC, Aaron J, Kurzrock R | title = Targeting the molecular chaperone heat shock protein 90 (HSP90): lessons learned and future directions | journal = Cancer Treatment Reviews | volume = 39 | issue = 4 | pages = 375–87 | date = Jun 2013 | pmid = 23199899 | doi = 10.1016/j.ctrv.2012.10.001 }}</ref> In [[salivary gland tumor]]s, expression of [[HSP90AA1]] and HSP90AB1 correlates with [[cancer|malignancy]],  [[cell growth|proliferation]] and [[metastasis]].<ref>{{cite journal | vauthors = Wang G, Gu X, Chen L, Wang Y, Cao B, E Q | title = Comparison of the expression of 5 heat shock proteins in benign and malignant salivary gland tumor tissues | journal = Oncology Letters | volume = 5 | issue = 4 | pages = 1363–1369 | date = Apr 2013 | pmid = 23599795 | doi = 10.3892/ol.2013.1166 | pmc=3629267}}</ref> The same is basically true for lung cancers where a correlation with survival was found.<ref>{{cite journal | vauthors = Biaoxue R, Xiling J, Shuanying Y, Wei Z, Xiguang C, Jinsui W, Min Z | title = Upregulation of Hsp90-beta and annexin A1 correlates with poor survival and lymphatic metastasis in lung cancer patients | journal = Journal of Experimental & Clinical Cancer Research | volume = 31 | pages = 70 | date = Aug 2012 | issue = 1 | pmid = 22929401 | doi = 10.1186/1756-9966-31-70 | pmc=3444906 | doi-access = free }}</ref>

==Notes==
{{Academic-written review|Q=Q38584468}}

== References ==
{{reflist|33em}}

== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Hoffmann T, Hovemann B | title = Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related genes encode formerly identified tumour-specific transplantation antigens | journal = Gene | volume = 74 | issue = 2 | pages = 491–501 | date = Dec 1988 | pmid = 2469626 | doi = 10.1016/0378-1119(88)90182-5 }}
* {{cite journal | vauthors = Lees-Miller SP, Anderson CW | title = Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II | journal = The Journal of Biological Chemistry | volume = 264 | issue = 5 | pages = 2431–7 | date = Feb 1989 | doi = 10.1016/S0021-9258(19)81631-9 | pmid = 2492519 | doi-access = free }}
* {{cite journal | vauthors = Rebbe NF, Ware J, Bertina RM, Modrich P, Stafford DW | title = Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family | journal = Gene | volume = 53 | issue = 2–3 | pages = 235–45 | year = 1987 | pmid = 3301534 | doi = 10.1016/0378-1119(87)90012-6 }}
* {{cite journal | vauthors = Tang PZ, Gannon MJ, Andrew A, Miller D | title = Evidence for oestrogenic regulation of heat shock protein expression in human endometrium and steroid-responsive cell lines | journal = European Journal of Endocrinology| volume = 133 | issue = 5 | pages = 598–605 | date = Nov 1995 | pmid = 7581991 | doi = 10.1530/eje.0.1330598 }}
* {{cite journal | vauthors = Nemoto T, Ohara-Nemoto Y, Ota M, Takagi T, Yokoyama K | title = Mechanism of dimer formation of the 90-kDa heat-shock protein | journal = European Journal of Biochemistry | volume = 233 | issue = 1 | pages = 1–8 | date = Oct 1995 | pmid = 7588731 | doi = 10.1111/j.1432-1033.1995.001_1.x | doi-access = free }}
* {{cite journal | vauthors = Takahashi I, Tanuma R, Hirata M, Hashimoto K | title = A cosmid clone at the D6S182 locus on human chromosome 6p12 contains the 90-kDa heat shock protein beta gene (HSP90 beta) | journal = Mammalian Genome | volume = 5 | issue = 2 | pages = 121–2 | date = Feb 1994 | pmid = 8180474 | doi = 10.1007/BF00292342 | s2cid = 30075426 }}
* {{cite journal | vauthors = Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ | title = A two-dimensional gel database of human colon carcinoma proteins | journal = Electrophoresis | volume = 18 | issue = 3–4 | pages = 605–13 | year = 1997 | pmid = 9150948 | doi = 10.1002/elps.1150180344 | s2cid = 25454450 }}
* {{cite journal | vauthors = Yano M, Naito Z, Yokoyama M, Shiraki Y, Ishiwata T, Inokuchi M, Asano G | title = Expression of hsp90 and cyclin D1 in human breast cancer | journal = Cancer Letters | volume = 137 | issue = 1 | pages = 45–51 | date = Mar 1999 | pmid = 10376793 | doi = 10.1016/S0304-3835(98)00338-3 }}
* {{cite journal | vauthors = Sato S, Fujita N, Tsuruo T | title = Modulation of Akt kinase activity by binding to Hsp90 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 20 | pages = 10832–7 | date = Sep 2000 | pmid = 10995457 | pmc = 27109 | doi = 10.1073/pnas.170276797 | bibcode = 2000PNAS...9710832S | doi-access = free }}
* {{cite journal | vauthors = Gisler SM, Stagljar I, Traebert M, Bacic D, Biber J, Murer H | title = Interaction of the type IIa Na/Pi cotransporter with PDZ proteins | journal = The Journal of Biological Chemistry | volume = 276 | issue = 12 | pages = 9206–13 | date = Mar 2001 | pmid = 11099500 | doi = 10.1074/jbc.M008745200 | s2cid = 35476933 | doi-access = free }}
* {{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
* {{cite journal | vauthors = King FW, Wawrzynow A, Höhfeld J, Zylicz M | title = Co-chaperones Bag-1, Hop and Hsp40 regulate Hsc70 and Hsp90 interactions with wild-type or mutant p53 | journal = The EMBO Journal | volume = 20 | issue = 22 | pages = 6297–305 | date = Nov 2001 | pmid = 11707401 | pmc = 125724 | doi = 10.1093/emboj/20.22.6297 }}
* {{cite journal | vauthors = Bouhouche-Chatelier L, Chadli A, Catelli MG | title = The N-terminal adenosine triphosphate binding domain of Hsp90 is necessary and sufficient for interaction with estrogen receptor | journal = Cell Stress & Chaperones | volume = 6 | issue = 4 | pages = 297–305 | date = Oct 2001 | doi = 10.1379/1466-1268(2001)006<0297:tntatb>2.0.co;2 | doi-broken-date = 1 November 2024 | pmid = 11795466 | pmc = 434412 }}
* {{cite journal | vauthors = Sato N, Yamamoto T, Sekine Y, Yumioka T, Junicho A, Fuse H, Matsuda T | title = Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3 | journal = Biochemical and Biophysical Research Communications | volume = 300 | issue = 4 | pages = 847–52 | date = Jan 2003 | pmid = 12559950 | doi = 10.1016/S0006-291X(02)02941-8 | hdl = 2115/28121 | s2cid = 1460250 | hdl-access = free }}
* {{cite journal | vauthors = Wu JM, Xiao L, Cheng XK, Cui LX, Wu NH, Shen YF | title = PKC epsilon is a unique regulator for hsp90 beta gene in heat shock response | journal = The Journal of Biological Chemistry | volume = 278 | issue = 51 | pages = 51143–9 | date = Dec 2003 | pmid = 14532285 | doi = 10.1074/jbc.M305537200 | doi-access =  free}}
* {{cite journal | vauthors = Nagaraja GM, Kandpal RP | title = Chromosome 13q12 encoded Rho GTPase activating protein suppresses growth of breast carcinoma cells, and yeast two-hybrid screen shows its interaction with several proteins | journal = Biochemical and Biophysical Research Communications | volume = 313 | issue = 3 | pages = 654–65 | date = Jan 2004 | pmid = 14697242 | doi = 10.1016/j.bbrc.2003.12.001 }}
* {{cite journal | vauthors = Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G | title = A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway | journal = Nature Cell Biology | volume = 6 | issue = 2 | pages = 97–105 | date = Feb 2004 | pmid = 14743216 | doi = 10.1038/ncb1086 | s2cid = 11683986 }}
{{refend}}

{{PDB Gallery|geneid=3326}}

{{Chaperones}}