プレクストリン相同領域、プレクストリン相同ドメイン
- 関
- PH domain
WordNet
- territory over which rule or control is exercised; "his domain extended into Europe"; "he made it the law of the land" (同)demesne, land
- (mathematics) the set of values of the independent variable for which a function is defined (同)domain of a function
- the quality of being similar or corresponding in position or value or structure or function
PrepTutorEJDIC
- (国の)領地,領土;(個人の)所有地 / (関心・活動などの)範囲,分野 / (個人・一族の)所有地 / (数学で)変域(関数の独立変数がとる値の集合)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/21 23:32:49」(JST)
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PH domain of tyrosine-protein kinase BTK
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| Identifiers |
| Symbol |
PH |
| Pfam |
PF00169 |
| InterPro |
IPR001849 |
| SMART |
PH |
| PROSITE |
PDOC50003 |
| SCOP |
1dyn |
| SUPERFAMILY |
1dyn |
| OPM superfamily |
51 |
| OPM protein |
1pls |
| CDD |
cd00821 |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
Pleckstrin homology domain (PH domain) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.[1][2][3][4][5][6][7]
This domain can bind Phosphatidylinositol lipids within biological membranes (such as Phosphatidylinositol (3,4,5)-trisphosphate and phosphatidylinositol (4,5)-bisphosphate),[8] and proteins such as the βγ-subunits of heterotrimeric G proteins,[9] and protein kinase C.[10] Through these interactions, PH domains play a role in recruiting proteins to different membranes, thus targeting them to appropriate cellular compartments or enabling them to interact with other components of the signal transduction pathways.
Contents
- 1 Lipid binding specificity
- 2 Structure
- 3 Proteins containing PH domain
- 4 Subfamilies
- 5 Examples
- 6 See also
- 7 References
- 8 External links
Lipid binding specificity
Individual PH domains possess specificities for phosphoinositides phosphorylated at different sites within the inositol ring, e.g., some bind phosphatidylinositol (4,5)-bisphosphate but not phosphatidylinositol (3,4,5)-trisphosphate or phosphatidylinositol (3,4)-bisphosphate, while others may possess the requisite affinity. This is important because it makes the recruitment of different PH domain containing proteins sensitive to the activities of enzymes that either phosphorylate or dephosphorylate these sites on the inositol ring, such as phosphoinositide 3-kinase or PTEN, respectively. Thus, such enzymes exert a part of their effect on cell function by modulating the localization of downstream signaling proteins that possess PH domains that are capable of binding their phospholipid products.
Structure
The 3D structure of several PH domains has been determined.[11] All known cases have a common structure consisting of two perpendicular anti-parallel beta sheets, followed by a C-terminal amphipathic helix. The loops connecting the beta-strands differ greatly in length, making the PH domain relatively difficult to detect while providing the source of the domain's specificity. The only conserved residue among PH domains is a single tryptophan located within the alpha helix that serves to nucleate the core of the domain.
Proteins containing PH domain
PH domains can be found in many different proteins, such as OSBP or ARF. Recruitment to the Golgi in this case is dependent on both PtdIns and ARF. A large number of PH domains have poor affinity for phosphoinositides and are hypothesized to function as protein binding domains. A Genome-wide look in Saccharomyces cerevisiae showed that most of the 33 yeast PH domains are indeed promiscuous in binding to phosphoinositides, while only one (Num1-PH) behaved highly specific .[12] Proteins reported to contain PH domains belong to the following families:
- Pleckstrin, the protein where this domain was first detected, is the major substrate of protein kinase C in platelets. Pleckstrin is one of the rare proteins to contain two PH domains.
- Ser/Thr protein kinases such as the Akt/Rac family, the beta-adrenergic receptor kinases, the mu isoform of PKC and the trypanosomal NrkA family.
- Tyrosine protein kinases belonging to the Btk/Itk/Tec subfamily.
- Insulin Receptor Substrate 1 (IRS-1).
- Regulators of small G-proteins like guanine nucleotide releasing factor GNRP (Ras-GRF) (which contains 2 PH domains), guanine nucleotide exchange proteins like vav, dbl, SoS and S. cerevisiae CDC24, GTPase activating proteins like rasGAP and BEM2/IPL2, and the human break point cluster protein bcr.
- Cytoskeletal proteins such as dynamin (see IPR001401), Caenorhabditis elegans kinesin-like protein unc-104 (see IPR001752), spectrin beta-chain, syntrophin (2 PH domains), and S. cerevisiae nuclear migration protein NUM1.
- Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see IPR000909) isoforms gamma and delta. Isoform gamma contains two PH domains, the second one is split into two parts separated by about 400 residues.
- Oxysterol-binding proteins OSBP, S. cerevisiae OSH1 and YHR073w.
- Mouse protein citron, a putative rho/rac effector that binds to the GTP-bound forms of rho and rac.
- Several S. cerevisiae proteins involved in cell cycle regulation and bud formation like BEM2, BEM3, BUD4 and the BEM1-binding proteins BOI2 (BEB1) and BOI1 (BOB1).
- C. elegans protein MIG-10.
- Ceramide kinase, a lipid kinase that phosphorylates ceramides to ceramide-1-phosphate.[13]
Subfamilies
- Spectrin/pleckstrin-like IPR001605
Examples
Human genes encoding proteins containing this domain include:
- ABR, ADRBK1, ADRBK2, AFAP, AFAP1, AFAP1L1, AFAP1L2, AKAP13, AKT1, AKT2, AKT3, ANLN, APBB1IP, APPL1, APPL2, ARHGAP10, ARHGAP12, ARHGAP15, ARHGAP21, ARHGAP22, ARHGAP23, ARHGAP24, ARHGAP25, ARHGAP26, ARHGAP27, ARHGAP9, ARHGEF16, ARHGEF18, ARHGEF19, ARHGEF2, ARHGEF3, ARHGEF4, ARHGEF5, ARHGEF6, ARHGEF7, ARHGEF9, ASEF2,
- BMX, BTK,
- C20orf42, C9orf100, CADPS, CADPS2, CDC42BPA, CDC42BPB, CDC42BPG, CENTA1, CENTA2, CENTB1, CENTB2, CENTB5, CENTD1, CENTD2, CENTD3, CENTG1, CENTG2, CENTG3, CIT, CNKSR1, CNKSR2, COL4A3BP, CTGLF1, CTGLF2, CTGLF3, * CTGLF4, CTGLF5, CTGLF6,
- DAB2IP, DAPP1, DDEF1, DDEF2, DDEFL1, DEF6, DEPDC2, DGKD, DGKH, DGKK, DNM1, DNM2, DNM3, DOCK10, DOCK11, DOCK9, DOK1, DOK2, DOK3, DOK4, DOK5, DOK6, DTGCU2,
- EXOC8,
- FAM109A, FAM109B, FARP1, FARP2, FGD1, FGD2, FGD3, FGD4, FGD5, FGD6,
- GAB1, GAB2, GAB3, GAB4, GRB10, GRB14, GRB7,
- IRS1, IRS2, IRS4, ITK, ITSN1, ITSN2,
- KALRN, KIF1A, KIF1B, KIF1Bbeta,
- MCF2, MCF2L, MCF2L2, MRIP, MYO10,
- NET1, NGEF,
- OBPH1, OBSCN, OPHN1, OSBP, OSBP2, OSBPL10, OSBPL11, OSBPL3, OSBPL5, OSBPL6, OSBPL7, OSBPL8, OSBPL9,
- PHLDA2, PHLDA3, PHLDB1, PHLDB2, PHLPP, PIP3-E, PLCD1, PLCD4, PLCG1, PLCG2, PLCH1, PLCH2, PLCL1, PLCL2, PLD1, PLD2, PLEK, PLEK2, PLEKHA1, PLEKHA2, PLEKHA3, PLEKHA4, PLEKHA5, PLEKHA6, PLEKHA7, PLEKHA8, PLEKHB1, PLEKHB2, PLEKHC1, PLEKHF1, PLEKHF2, PLEKHG1, PLEKHG2, PLEKHG3, PLEKHG4, PLEKHG5, PLEKHG6, PLEKHH1, PLEKHH2, PLEKHH3, PLEKHJ1, PLEKHK1, PLEKHM1, PLEKHM2, PLEKHO1, PLEKHQ1, PREX1, PRKCN, PRKD1, PRKD2, PRKD3, PSCD1, PSCD2, PSCD3, PSCD4, PSD, PSD2, PSD3, PSD4, RALGPS1, RALGPS2, RAPH1,
- RASA1, RASA2, RASA3, RASA4, RASAL1, RASGRF1, RGNEF, ROCK1, ROCK2, RTKN,
- SBF1, SBF2, SCAP2, SGEF, SH2B, SH2B1, SH2B2, SH2B3, SH3BP2, SKAP1, SKAP2, SNTA1, SNTB1, SNTB2, SOS1, SOS2, SPATA13, SPNB4, SPTBN1, SPTBN2, SPTBN4, SPTBN5, STAP1, SWAP70, SYNGAP1,
- TBC1D2, TEC, TIAM1, TRIO, TRIOBP, TYL,
- URP1, URP2,
- VAV1, VAV2, VAV3, VEPH1
See also
- Pleckstrin
- The unrelated FYVE domain binds Phosphatidylinositol 3-phosphate and has been found in over 60 proteins.
- The GRAM domain is a structurally related protein domain.
References
- ^ Mayer, B. J.; Ren, R.; Clark, K. L.; Baltimore, D. (1993). "A putative modular domain present in diverse signaling proteins". Cell 73 (4): 629–630. doi:10.1016/0092-8674(93)90244-K. PMID 8500161. edit
- ^ Haslam, R. J.; Koide, H. B.; Hemmings, B. A. (1993). "Pleckstrin domain homology". Nature 363 (6427): 309. doi:10.1038/363309b0. edit
- ^ Musacchio, A.; Gibson, T.; Rice, P.; Thompson, J.; Saraste, M. (1993). "The PH domain: A common piece in the structural pathcwork of signalling proteins". Trends in Biochemical Sciences 18 (9): 343–348. doi:10.1016/0968-0004(93)90071-T. PMID 8236453. edit
- ^ Gibson, T. J.; Hyvönen, M.; Musacchio, A.; Saraste, M.; Birney, E. (1994). "PH domain: The first anniversary". Trends in Biochemical Sciences 19 (9): 349–353. doi:10.1016/0968-0004(94)90108-2. PMID 7985225. edit
- ^ Pawson, T. (1995). "Protein modules and signalling networks". Nature 373 (6515): 573–580. doi:10.1038/373573a0. PMID 7531822. edit
- ^ Ingley, E.; Hemmings, B. A. (1994). "Pleckstrin homology (PH) domains in signal transducton". Journal of Cellular Biochemistry 56 (4): 436–443. doi:10.1002/jcb.240560403. PMID 7890802. edit
- ^ Saraste, M.; Hyvönen, M. (1995). "Pleckstrin homology domains: A fact file". Current Opinion in Structural Biology 5 (3): 403–408. doi:10.1016/0959-440X(95)80104-9. PMID 7583640. edit
- ^ Wang, D. S.; Shaw, G. (1995). "The Association of the C-Terminal Region of β1ΣII Spectrin to Brain Membranes is Mediated by a pH Domain, Does Not Require Membrane Proteins, and Coincides with a Inositol-1,4,5 Trisphosphate Binding Site". Biochemical and Biophysical Research Communications 217 (2): 608–615. doi:10.1006/bbrc.1995.2818. PMID 7503742. edit
- ^ Wang, D. S.; Shaw, R.; Winkelmann, J. C.; Shaw, G. (1994). "Binding of PH Domains of β-Adrenergic-Receptor Kinase and β-Spectrin to WD40/β-Transducin Repeat Containing Regions of the β-Subunit of Trimeric G-Proteins". Biochemical and Biophysical Research Communications 203 (1): 29–35. doi:10.1006/bbrc.1994.2144. PMID 8074669. edit
- ^ Yao, L.; Kawakami, Y.; Kawakami, T. (1994). "The pleckstrin homology domain of Bruton tyrosine kinase interacts with protein kinase C". Proceedings of the National Academy of Sciences 91 (19): 9175. doi:10.1073/pnas.91.19.9175. edit
- ^ Riddihough, G. (1994). "More meanders and sandwiches". Nature Structural Biology 1 (11): 755–757. doi:10.1038/nsb1194-755. PMID 7634082. edit
- ^ Yu, J. W.; Mendrola, J. M.; Audhya, A.; Singh, S.; Keleti, D.; Dewald, D. B.; Murray, D.; Emr, S. D.; Lemmon, M. A. (2004). "Genome-Wide Analysis of Membrane Targeting by S. Cerevisiae Pleckstrin Homology Domains". Molecular Cell 13 (5): 677–688. doi:10.1016/S1097-2765(04)00083-8. PMID 15023338. edit
- ^ Sugiura, M.; Kono, K.; Liu, H.; Shimizugawa, T.; Minekura, H.; Spiegel, S.; Kohama, T. (2002). "Ceramide Kinase, a Novel Lipid Kinase. MOLECULAR CLONING AND FUNCTIONAL CHARACTERIZATION". Journal of Biological Chemistry 277 (26): 23294–23300. doi:10.1074/jbc.M201535200. PMID 11956206. edit
External links
- Nash Lab Protein Interaction Domains - PH domain description
- UMich Orientation of Proteins in Membranes families/superfamily-51 - Calculated orientations of PH domains in membranes
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Protein domains
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- BAR
- BIR
- BZIP
- CARD
- C1
- C2
- DED
- ENTH
- FYVE
- HEAT
- Kringle
- LIM
- LRR
- NACHT
- PAS
- PDZ
- Pyrin
- PH
- PX
- SH2
- SH3
- SUN
- TRIO
- WD40
- zinc finger
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Index of genetics
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| Description |
- Gene expression
- DNA
- replication
- cycle
- recombination
- repair
- binding proteins
- Transcription
- factors
- regulators
- nucleic acids
- RNA
- RNA binding proteins
- ribonucleoproteins
- repeated sequence
- modification
- Translation
- ribosome
- modification
- nexins
- Proteins
- domains
- Structure
- primary
- secondary
- tertiary
- quaternary
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| Disease |
- Replication and repair
- Transcription factor
- Transcription
- Translation
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UpToDate Contents
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English Journal
- Phosphatidic Acid-Mediated Signaling Regulates Microneme Secretion in Toxoplasma.
- Bullen HE1, Jia Y1, Yamaryo-Botté Y2, Bisio H1, Zhang O3, Jemelin NK1, Marq JB1, Carruthers V3, Botté CY2, Soldati-Favre D4.
- Cell host & microbe.Cell Host Microbe.2016 Mar 9;19(3):349-60. doi: 10.1016/j.chom.2016.02.006.
- The obligate intracellular lifestyle of apicomplexan parasites necessitates an invasive phase underpinned by timely and spatially controlled secretion of apical organelles termed micronemes. In Toxoplasma gondii, extracellular potassium levels and other stimuli trigger a signaling cascade culminatin
- PMID 26962945
- Adiponectin Promotes Human Jaw Bone Marrow Stem Cell Osteogenesis.
- Pu Y1, Wu H1, Lu S2, Hu H2, Li D2, Wu Y3, Tang Z2.
- Journal of dental research.J Dent Res.2016 Mar 9. pii: 0022034516636853. [Epub ahead of print]
- Human jaw bone marrow mesenchymal stem cells (h-JBMMSCs) are multipotent progenitor cells with osteogenic differentiation potential. The relationship between adiponectin (APN) and the metabolism of h-JBMMSCs has not been fully elucidated, and the underlying mechanism remains unclear. The aim of the
- PMID 26961489
- MicroRNA-181b Improves Glucose Homeostasis and Insulin Sensitivity by Regulating Endothelial Function in White Adipose Tissue.
- Sun X1, Lin J1, Zhang Y1, Kang S1, Belkin N1, Wara AK1, Icli B1, Hamburg NM1, Li D1, Feinberg MW2.
- Circulation research.Circ Res.2016 Mar 4;118(5):810-21. doi: 10.1161/CIRCRESAHA.115.308166. Epub 2016 Jan 7.
- RATIONALE: The pathogenesis of insulin resistance involves dysregulated gene expression and function in multiple cell types, including endothelial cells (ECs). Post-transcriptional mechanisms such as microRNA-mediated regulation of gene expression could affect insulin action by modulating EC functio
- PMID 26830849
Japanese Journal
- Role of FGD1, a Cdc42 Guanine Nucleotide Exchange Factor, in Epidermal Growth Factor-Stimulated c-Jun NH2-Terminal Kinase Activation and Cell Migration
- Oshima Toshiyuki,Fujino Tomofumi,Ando Ken,Hayakawa Makio
- Biological & Pharmaceutical Bulletin 34(1), 54-60, 2011
- … While most mutations were found in the catalytic region, which consists of Dbl homology (DH) domain and adjacent pleckstrin homology (PH) domain, a missense mutation in the proline-rich domain is also found in a patient with typical clinical features as AAS. … Here we show that the proline-rich domain is critical for FGD1-induced directionally persistent cell migration. …
- NAID 130000402262
- Interactions of STAP-2 with Brk and STAT3 participate in cell growth of human breast cancer cells.
- Ikeda Osamu,Sekine Yuichi,Mizushima Akihiko,Nakasuji Misa,Miyasaka Yuto,Yamamoto Chikako,Muromoto Ryuta,Nanbo Asuka,Oritani Kenji,Yoshimura Akihiko,Matsuda Tadashi
- The Journal of Biological Chemistry 285(49), 38093-38103, 2010-12-06
- … Signal transducing adaptor protein-2 (STAP-2) is a recently identified adaptor protein, which contains pleckstrin homology (PH) and Src homology 2 (SH2)-like domains, as well as a signal transducer and an activator of transcription 3 (STAT3)-binding motif in its C-terminal region. … The PH domain of STAP-2 is involved in multiple steps; …
- NAID 120002646845
Related Links
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★リンクテーブル★
[★]
- 英
- pleckstrin homology domain、PH domain
- 関
- PHドメイン、プレクストリン相同領域
[★]
PHドメイン、プレクストリン相同ドメイン
- 関
- pleckstrin homology domain
[★]
- 英
- pleckstrin homology domain
- 関
- プレクストリン相同ドメイン
[★]
- 関
- area、realm、region、regional、segregation、territory、universe
[★]
- 関
- homologous region、homology region
[★]
- 関
- homologous
[★]
- 関
- homologue
[★]
- 関
- See also specific type