Hormone receptor - wikipedia Hormone receptor A hormone receptor is a receptor molecule that binds to a specific hormone. Hormone receptors are a wide family of proteins made up of receptors for thyroid and steroid hormones, retinoids and Vitamin D, and a variety of other receptors for various ligands, such as fatty acids and prostaglandins. There are two main classes of hormone receptors. Receptors for peptide hormones tend to be cell surface receptors built into the plasma membrane of cells and are thus referred to as trans membrane receptors. An example of this is insulin. Receptors for steroid hormones are usually found within the cytoplasm and are referred to as intracellular or nuclear receptors, such as testosterone. Upon hormone binding, the receptor can initiate multiple signaling pathways which ultimately lead to changes in the behavior of the target cells. Hormonal therapy and hormone receptors play a very large part in breast cancer treatment ( therapy is not limited to only breast cancer ). By influencing the hormones, the cells ' growth can be changed along with its function. These hormones can cause cancer to not survive in the human body. Contents 1 General Ligand Binding 2 Functions 2.1 Transmission of Signal 2.1. 1 Intracellular ( Nuclear Receptors ) 2.1. 2 Trans - Membrane Receptors 2.2 Aiding Gene Expression 3 Classification 3.1 Receptors for water - soluble hormones 3.2 Receptors for lipid - soluble hormones 4 List of hormone receptors 5 References General ligand binding Signal molecule binds to its hormone receptor, inducing a conformational change in the receptor to begin a signaling cascade that will induce a cellular response. Hormone receptor proteins bind to a hormone as a result of an accumulation of weak interactions. Because of the relatively large size of enzymes and receptors, the large amount of surface area provides the basis for these weak interactions to occur. This binding is actually highly specific because of the complementarity of these interactions between polar, non-polar, charged, neutral, hydrophilic, or hydrophobic residues. Upon binding, the receptor often undergoes a conformational change and may bind further signaling ligands in order to activate a signaling pathway. Because of these highly specific and high affinity interactions between hormones and their receptors, very low concentrations of hormone are needed to produce significant cellular response. Receptors can have various different structures depending on the function of the hormone and the structure of its ligand. Therefore, hormone binding to its receptor is a complex process which can be mediated by cooperative binding, reversible and irreversible interactions, and multiple binding sites. Functions Transmission of signal The presence of hormone or multiple hormones enables a response in the receptor which begins a cascade of signaling. The hormone receptor interacts with different molecules in order to induce a variety of changes, such as the increase or decrease of nutrient sources, growth, and other metabolic functions. These signaling pathways are complex mechanisms mediated by feedback loops where different signals activate and inhibit other signals. If a signaling pathway ends with the increase in production of a nutrient, that nutrient is then a signal back to the receptor that acts as a competitive inhibitor to prevent further production. Signaling pathways regulate cells through activating or inactivating gene expression, transport of metabolites, and controlling enzymatic activity in order to manage growth and functions of metabolism. Intracellular ( nuclear receptors ) Intracellular and nuclear receptors are a direct way for the cell to respond to internal changes and signals. Intracellular receptors are activated by hydrophobic ligands which pass through the cellular membrane. All nuclear receptors are very similar in structure, and are described with intrinsic transcriptional activity. Intrinsic transcriptional involves the three following domains : transcription - activating, DNA - binding, and ligand - binding. These domains and ligands are hydrophobic and are able to travel through the membrane. The movement of macromolecules and ligand molecules into the cell enables a complex transport system of intracellular signal transfers through different cellular environments until response is enabled. Nuclear receptors are a special class of intracellular receptor which specifically aid the needs of the cell to express certain genes. Nuclear receptors often bind directly to DNA by targeting specific DNA sequences in order to express or repress transcription of nearby genes. Trans - membrane receptors The extracellular environment is able to induce changes within the cell. Hormones, or other extracellular signals, are able to induce changes within the cell by binding to membrane - bound receptors. This interaction allows the hormone receptor to produce second messengers within the cell to aid response. Second messengers may also be sent to interact with intracellular receptors in order to enter the complex signal transport system that eventually changes cellular function. Aiding gene expression Hormone receptors can behave as transcription factors by interacting directly with DNA or by cross-talking with signaling pathways. This process is mediated through co-regulators. In the absence of ligand, receptor molecules bind corepressors in order to repress gene expression, compacting chromatin through histone deacetylatase. When a ligand is present, nuclear receptors undergo a conformational change to recruit various coactivators. These molecules work to remodel chromatin. Hormone receptors have highly specific motifs which are able to interact with coregulator complexes. This is the mechanism through which receptors can induce regulation of gene expression depending on both the extracellular environment and the immediate cellular composition. Steroid hormones and their regulation by receptors are the most potent molecule interactions in aiding gene expression. Problems with nuclear receptor binding as a result of shortages of ligand or receptors can have drastic effects on the cell. The dependency on the ligand is the most important part in being able to regulate gene expression, so the absence of ligand is drastic to this process. For example, estrogen deficiency is a cause of osteoporosis and the inability to undergo a proper signaling cascade prevents bone growth and strengthening. Deficiencies in nuclear receptor - mediated pathways play a key role in the development of disease, like osteoporosis. Classification Receptors for water - soluble hormones Water - soluble hormones include glycoproteins, catecholamines, and peptide hormones composed of polypeptides, e.g. thyroid - stimulating hormone, follicle - stimulating hormone, luteinizing hormone and insulin. These molecules are not lipid - soluble and therefore can not diffuse through cell membranes. Consequently, receptors for peptide hormones are located on the plasma membrane because they have bound to a receptor protein located on the plasma membrane. Water - soluble hormones come from amino acids and are located and stored in endocrine cells until actually needed. The main two types of transmembrane receptor hormone receptor are the G - protein - coupled receptors and the enzyme - linked receptors. These receptors generally function via intracellular second messengers, including cyclic AMP ( cAMP ), cyclic GMP ( cGMP ), inositol 1, 4, 5 - trisphosphate ( IP3 ) and the calcium ( Ca ) - calmodulin system. Receptors for lipid - soluble hormones Cartoon representation of the human hormone estrogen receptor DBD. DNA = Orange and Blue. DBD of Estrogen Receptor = white. Zinc Atoms = Green. Steroid hormone receptors and related receptors are generally soluble proteins that function through gene activation. Lipid - soluble hormones target specific sequences of DNA by diffusing into the cell. When they have diffused into the cell, they bind to receptors ( intracellular ), and migrate into the nucleus. heir response elements are DNA sequences ( promoters ) that are bound by the complex of the steroid bound to its receptor. The receptors themselves are zinc - finger proteins. These receptors include those for glucocorticoids ( glucocorticoid receptors ), estrogens ( estrogen receptors ), androgens ( androgen receptors ), thyroid hormone ( T3 ) ( thyroid hormone receptors ), calcitriol ( the active form of vitamin D ) ( calcitriol receptors ), and the retinoids ( vitamin A ) ( retinoid receptors ). Receptor - protein interactions induce the uptake and destruction of their respective hormones in order to regulate their concentration in the body. This is especially important for steroid hormones because many body systems are entirely steroid dependent. List of hormone receptors This list is incomplete ; you can help by expanding it. For some of these classes, in any given species ( such as, for example, humans ), there is a single molecule encoded by a single gene ; in other cases, there are several molecules in the class. Androgen receptors Calcitriol receptors Corticotropin - releasing hormone receptor 1 Corticotropin releasing hormone receptor 2 Estrogen receptors Follicle - stimulating hormone receptors Glucagon receptors Gonadotropin receptors Gonadotropin - releasing hormone receptors Growth hormone receptors Luteinizing hormone Progesterone receptors Retinoid receptors Somatostatin receptors Thyroid hormone receptors Thyrotropin receptors References ^ Jump up to : Aranda, A. ; Pascual, A. ( 2001 - 07 - 01 ). `` Nuclear hormone receptors and gene expression ''. Physiological Reviews. 81 ( 3 ) : 1269 -- 1304. doi : 10.1152 / physrev. 2001.81. 3.1269. ISSN 0031 - 9333. PMID 11427696. ^ Jump up to : Gammeltoft, S. ( 1984 - 10 - 01 ). `` Insulin receptors : binding kinetics and structure - function relationship of insulin ''. Physiological Reviews. 64 ( 4 ) : 1321 -- 1378. ISSN 0031 - 9333. PMID 6387730. Jump up ^ McEwen, B.S. ; Kloet, E.R. De ; Rostene, W. ( 1986 - 10 - 01 ). `` Adrenal steroid receptors and actions in the nervous system ''. Physiological Reviews. 66 ( 4 ) : 1121 -- 1188. ISSN 0031 - 9333. PMID 3532143. Jump up ^ `` Understanding Hormone Receptors and What They Do ''. Breastcancer.org. Retrieved 2017 - 04 - 06. ^ Jump up to : Nelson 1, Cox 2, Lehninger 3. Principles of Biochemistry. New York : Worth. p. 81. CS1 maint : Multiple names : authors list ( link ) Jump up ^ Mullur, Rashmi ; Liu, Yan - Yun ; Brent, Gregory A. ( 2014 - 04 - 01 ). `` Thyroid Hormone Regulation of Metabolism ''. Physiological Reviews. 94 ( 2 ) : 355 -- 382. doi : 10.1152 / physrev. 00030.2013. ISSN 0031 - 9333. PMC 4044302. PMID 24692351. Jump up ^ Argetsinger, L.S. ; Carter - Su, C. ( 1996 - 10 - 01 ). `` Mechanism of signaling by growth hormone receptor ''. Physiological Reviews. 76 ( 4 ) : 1089 -- 1107. ISSN 0031 - 9333. PMID 8874495. Jump up ^ `` Mechanism of Action : Hormones with Intracellular Receptors ''. www.vivo.colostate.edu. Retrieved 2017 - 04 - 06. Jump up ^ `` Molecular Biology ''. www.uh.edu. Retrieved 2017 - 04 - 06. Jump up ^ Follis, Ariele Viacava ; Llambi, Fabien ; Ou, Li ; Baran, Katherine ; Green, Douglas R. ; Kriwacki, Richard W. ( 2014 - 06 - 01 ). `` The DNA - binding domain mediates both nuclear and cytosolic functions of p53 ''. Nature Structural & Molecular Biology. 21 ( 6 ) : 535 -- 543. doi : 10.1038 / nsmb. 2829. ISSN 1545 - 9993. PMC 4134560. PMID 24814347. Jump up ^ `` Ligand Binding Domain ''. www.ks.uiuc.edu. Retrieved 2017 - 04 - 06. Jump up ^ `` Cell signalling ''. OpenLearn. Retrieved 2017 - 04 - 06. Jump up ^ Stockert, R.J. ( 1995 - 07 - 01 ). `` The asialoglycoprotein receptor : relationships between structure, function, and expression ''. Physiological Reviews. 75 ( 3 ) : 591 -- 609. ISSN 0031 - 9333. PMID 7624395. Jump up ^ Vasudevan, Nandini ; Ogawa, Sonoko ; Pfaff, Donald ( 2002 - 01 - 10 ). `` Estrogen and Thyroid Hormone Receptor Interactions : Physiological Flexibility by Molecular Specificity ''. Physiological Reviews. 82 ( 4 ) : 923 -- 944. doi : 10.1152 / physrev. 00014.2002. ISSN 0031 - 9333. PMID 12270948. Jump up ^ Imai, Yuuki ; Youn, Min - Young ; Inoue, Kazuki ; Takada, Ichiro ; Kouzmenko, Alexander ; Kato, Shigeaki ( 2013 - 04 - 01 ). `` Nuclear Receptors in Bone Physiology and Diseases ''. Physiological Reviews. 93 ( 2 ) : 481 -- 523. doi : 10.1152 / physrev. 00008.2012. ISSN 0031 - 9333. PMC 3768103. PMID 23589826. Jump up ^ Boundless ( 2016 - 10 - 23 ). `` Mechanisms of Hormone Action ''. Boundless. Jump up ^ `` e. hormone Endocrine System : Types of Hormones ''. e.hormone.tulane.edu. Retrieved 2017 - 04 - 06. Jump up ^ `` The Endocrine System ''. classes.midlandstech.edu. Retrieved 2017 - 04 - 06. Jump up ^ Steroid Hormone Receptors and their Response Elements Jump up ^ Gimpl, Gerald ; Fahrenholz, Falk ( 2001 - 04 - 01 ). `` The Oxytocin Receptor System : Structure, Function, and Regulation ''. Physiological Reviews. 81 ( 2 ) : 629 -- 683. ISSN 0031 - 9333. PMID 11274341. Jump up ^ `` Luteinizing hormone ''. Wikipedia. 2017 - 03 - 15. Neuropeptide receptors G protein - coupled receptor Hormone receptors Hypothalamic CRH FSH LHRH TRH Somatostatin Pituitary Vasopressin 1A 1B Oxytocin LHCG TSH Other Atrial natriuretic factor NPR3 Calcitonin Cholecystokinin VIP Opioid receptors Delta Kappa Mu Nociceptin Other neuropeptide receptors Angiotensin Bradykinin B1 B2 Tachykinin TACR1 Calcitonin gene - related peptide Galanin GPCR neuropeptide B / W FF Y Neurotensin Type I cytokine receptor GH Prolactin Enzyme - linked receptor Atrial natriuretic factor NPR1 NPR2 Other Sigma Transcription factors and intracellular receptors ( 1 ) Basic domains ( 1.1 ) Basic leucine zipper ( bZIP ) Activating transcription factor AATF 5 6 7 AP - 1 c - Fos FOSB FOSL1 FOSL2 JDP2 c - Jun JUNB JunD BACH BATF BLZF1 C / EBP α β γ δ ε ζ CREB L1 CREM DBP DDIT3 GABPA GCN4 HLF MAF NFE L1 L2 L3 NFIL3 NRL NRF XBP1 ( 1.2 ) Basic helix - loop - helix ( bHLH ) ATOH1 AhR AHRR ARNT ASCL1 BHLH 9 ARNTL ARNTL ARNTL2 CLOCK EPAS1 FIGLA HAND HES 5 6 HEY HES1 HIF 1A 3A ID LYL1 MESP2 MXD4 MYCL1 MYCN Myogenic regulatory factors MyoD Myogenin MYF5 MYF6 Neurogenins NeuroD NPAS OLIG Pho4 Scleraxis SIM TAL Twist USF1 ( 1.3 ) bHLH - ZIP AP - 4 MAX MXD3 MITF MNT MLX MXI1 Myc SREBP ( 1.4 ) NF - 1 NFI X SMAD R - SMAD 5 9 I - SMAD 6 7 4 ) ( 1.5 ) RF - X RFX 5 6 ANK ( 1.6 ) Basic helix - span - helix ( bHSH ) AP - 2 α β γ δ ε hide ( 2 ) Zinc finger DNA - binding domains ( 2.1 ) Nuclear receptor ( Cys ) subfamily 1 Thyroid hormone α β CAR FXR LXR α β PPAR α β / δ γ PXR RAR α β γ ROR α β γ Rev - ErbA α β VDR subfamily 2 COUP - TF ( I II Ear - 2 HNF4 α γ PNR RXR α β γ Testicular receptor TLX subfamily 3 Steroid hormone Androgen Estrogen α β Glucocorticoid Mineralocorticoid Progesterone Estrogen related α β γ subfamily 4 NUR NGFIB NOR1 NURR1 subfamily 5 LRH - 1 SF1 subfamily 6 GCNF subfamily 0 DAX1 SHP ( 2.2 ) Other Cys GATA 5 6 MTA TRPS1 ( 2.3 ) Cys His General transcription factors TFIIA TFIIB TFIID TFIIE TFIIF TFIIH 2I 3A 3C1 3C2 ATBF1 BCL 6 11A 11B CTCF E4F1 EGR ERV3 GFI1 GLI - Krüppel family REST S1 S2 YY1 HIC HIVEP IKZF ILF KLF 5 6 7 8 9 10 11 12 13 14 15 17 MTF1 MYT1 OSR1 PRDM9 SALL SP 7 8 TSHZ3 WT1 Zbtb7 7A 7B ZBTB 11 16 17 20 32 33 40 zinc finger 7 9 10 19 22 24 33B 34 35 41 43 44 51 74 143 146 148 165 202 217 219 238 239 259 267 268 281 295 300 318 330 346 350 365 366 384 423 451 452 471 593 638 644 649 655 ( 2.4 ) Cys HIVEP1 ( 2.5 ) Alternating composition AIRE DIDO1 GRLF1 ING JARID 1A 1B 1C 1D JMJD1B ( 2.6 ) WRKY WRKY ( 3 ) Helix - turn - helix domains ( 3.1 ) Homeodomain ARX CDX CRX CUTL1 DBX DLX 5 6 EMX EN FHL HESX1 HHEX HLX Homeobox A1 A2 A3 A4 A5 A7 A9 A10 A11 A13 B1 B2 B3 B4 B5 B6 B7 B8 B9 B13 C4 C5 C6 C8 C9 C10 C11 C12 C13 D1 D3 D4 D8 D9 D10 D11 D12 D13 HOPX IRX 5 6 MKX LMX 1A 1B MEIS MEOX2 MNX1 MSX NANOG NKX 2 - 1 2 - 2 2 - 3 2 - 5 3 - 1 3 - 2 6 - 1 6 - 2 NOBOX PBX PHF 6 8 10 16 17 20 21A PHOX 2A 2B PITX POU domain PIT - 1 BRN - 3 : A Octamer transcription factor : 1 3 / 4 6 7 11 OTX PDX1 SATB2 SHOX2 SIX 5 VAX1 ZEB ( 3.2 ) Paired box PAX 5 6 7 8 9 PRRX RAX ( 3.3 ) Fork head / winged helix E2F 5 FOX proteins A1 A2 A3 C1 C2 D3 D4 E1 E3 F1 G1 H1 I1 J1 J2 K1 K2 L2 M1 N1 N3 O1 O3 O4 P1 P2 P3 P4 ( 3.4 ) Heat shock factors HSF ( 3.5 ) Tryptophan clusters ELF 5 EGF ELK ERF ETS ERG SPIB ETV 5 6 FLI1 Interferon regulatory factors 5 6 7 8 MYB MYBL2 ( 3.6 ) TEA domain transcriptional enhancer factor ( 4 ) β - Scaffold factors with minor groove contacts ( 4.1 ) Rel homology region NF - κB NFKB1 NFKB2 REL RELA RELB NFAT C1 C2 C3 C4 5 ( 4.2 ) STAT STAT 5 6 ( 4.3 ) p53 p53 TBX 5 19 21 22 TBR1 TBR2 TFT MYRF TP63 ( 4.4 ) MADS box Mef2 SRF ( 4.6 ) TATA - binding proteins TBP TBPL1 ( 4.7 ) High - mobility group BBX HMGB HMGN HNF 1A 1B LEF1 SOX 5 6 8 9 10 11 12 13 14 15 18 21 SRY SSRP1 TCF TOX ( 4.9 ) Grainyhead TFCP2 ( 4.10 ) Cold - shock domain CSDA YBX1 ( 4.11 ) Runt CBF CBFA2T2 CBFA2T3 RUNX1 RUNX2 RUNX3 RUNX1T1 ( 0 ) Other transcription factors ( 0.2 ) HMGI ( Y ) HMGA HBP1 ( 0.3 ) Pocket domain Rb RBL1 RBL2 ( 0.5 ) AP - 2 / EREBP - related factors Apetala 2 EREBP B3 ( 0.6 ) Miscellaneous ARID 1A 1B 3A 3B 4A CAP IFI 16 35 MLL T1 MNDA NFY Rho / Sigma see also transcription factor / coregulator deficiencies Retrieved from `` https://en.wikipedia.org/w/index.php?title=Hormone_receptor&oldid=831026514 '' Categories : Receptors Integral membrane proteins Hidden categories : CS1 maint : Multiple names : authors list Incomplete lists from March 2016 Talk Contents About Wikipedia Dansk Deutsch Français Italiano Српски / srpski Srpskohrvatski / српскохрватски Edit links This page was last edited on 18 March 2018, at 08 : 55. 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Question: which type of hormone receptor plasma membrane bound or intracellular
Answer: intracellular