PHドメイン、プレクストリン相同ドメイン
- 関
- pleckstrin homology 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
- (from potential of Hydrogen) the logarithm of the reciprocal of hydrogen-ion concentration in gram atoms per liter; provides a measure on a scale from 0 to 14 of the acidity or alkalinity of a solution (where 7 is neutral and greater than 7 is more basic and less than 7 is more acidic); (同)pH scale
- the 16th letter of the Roman alphabet (同)p
- a river in western Thailand; a major tributary of the Chao Phraya (同)Ping River
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)
- ペーハー(水素イオン濃度指数)
- parking
- phosphorusの化学記号
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/01/04 00:37:22」(JST)
[Wiki en表示]
|
PH domain of tyrosine-protein kinase BTK
|
| 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 InterPro: IPR001401), Caenorhabditis elegans kinesin-like protein unc-104 (see InterPro: IPR001752), spectrin beta-chain, syntrophin (2 PH domains), and S. cerevisiae nuclear migration protein NUM1.
- Mammalian phosphatidylinositol-specific phospholipase C (PI-PLC) (see InterPro: 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 InterPro: 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.
- ^ Haslam, R. J.; Koide, H. B.; Hemmings, B. A. (1993). "Pleckstrin domain homology". Nature. 363 (6427): 309–10. doi:10.1038/363309b0. PMID 8497315.
- ^ 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.
- ^ 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.
- ^ Pawson, T. (1995). "Protein modules and signalling networks". Nature. 373 (6515): 573–580. doi:10.1038/373573a0. PMID 7531822.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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): 9175–9179. doi:10.1073/pnas.91.19.9175.
- ^ Riddihough, G. (1994). "More meanders and sandwiches". Nature Structural Biology. 1 (11): 755–757. doi:10.1038/nsb1194-755. PMID 7634082.
- ^ 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.
- ^ 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.
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
|
Protein domains
|
|
- 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
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Stimuli-enabled zipper-like graphene interface for auto-switchable bioelectronics.
- Mishra S1, Ashaduzzaman M2, Mishra P1, Swart HC3, Turner AP4, Tiwari A5.
- Biosensors & bioelectronics.Biosens Bioelectron.2017 Mar 15;89(Pt 1):305-311. doi: 10.1016/j.bios.2016.03.052. Epub 2016 Mar 22.
- Graphene interfaces with multi-stimuli responsiveness are of particular interest due to their diverse super-thin interfacial behaviour, which could be well suited to operating complex physiological systems in a single miniaturised domain. In general, smart graphene interfaces switch bioelectrodes fr
- PMID 27132998
- Investigation by response surface methodology of the combined effect of pH and composition of water-methanol mixtures on the stability of curcuminoids.
- D'Archivio AA1, Maggi MA2.
- Food chemistry.Food Chem.2017 Mar 15;219:414-418. doi: 10.1016/j.foodchem.2016.09.167. Epub 2016 Sep 28.
- Response surface methodology, coupled to a full factorial three-level experimental design, was applied to investigate the combined influence of pH (between 7.0 and 8.6) and composition of methanol-water mixtures (between 30 and 70% v/v of methanol content) on the stability of curcumin and its analog
- PMID 27765246
- Interdomain electron transfer in cellobiose dehydrogenase is governed by surface electrostatics.
- Kadek A1, Kavan D1, Marcoux J2, Stojko J2, Felice AK3, Cianférani S2, Ludwig R3, Halada P4, Man P5.
- Biochimica et biophysica acta.Biochim Biophys Acta.2017 Feb;1861(2):157-167. doi: 10.1016/j.bbagen.2016.11.016. Epub 2016 Nov 13.
- BACKGROUND: Cellobiose dehydrogenase (CDH) is a fungal extracellular oxidoreductase which fuels lytic polysaccharide monooxygenase with electrons during cellulose degradation. Interdomain electron transfer between the flavin and cytochrome domain in CDH, preceding the electron flow to lytic polysacc
- PMID 27851982
Japanese Journal
- The Effects of Internal and Receptor pH on the Rate of Drug Release from Water-in-Oil Emulsions
- Fujihira Atsushi,Shimizu Nobuaki
- Chemical and Pharmaceutical Bulletin 62(1), 64-71, 2014
- … We evaluated the effects of internal phase and receptor solution pH on the rate of drug release from water-in-oil emulsions using methylene blue as a model drug. … The methylene blue release rate was strongly dependent on both internal phase and receptor solution pH. Methylene blue dissolved in squalene in the presence of a surfactant. … The water–squalene distribution of methylene blue changed with pH, whereas its ionic state did not. …
- NAID 130003381807
- Novel Small-Molecule Compounds That Affect Cellular Morphogenesis in Yeast and Mammalian Cells
- FUKUNAGA Tomoaki,NAKAMURA Mikiko,KITAGAWA Takao [他]
- Bioscience, Biotechnology, and Biochemistry 77(8), 1669-1676, 2013-08
- NAID 40019760019
- EFA6 activates Arf6 and participates in its targeting to the Flemming body during cytokinesis.
- Ueda Tomoko,Hanai Ayako,Takei Tomomi,Kubo Keiji,Ohgi Minako,Sakagami Hiroyuki,Takahashi Senye,Shin Hye-Won,Nakayama Kazuhisa
- FEBS letters 587(11), 1617-1623, 2013-06-05
- … Here, we show that EFA6 (exchange factor for Arf6) localizes on the cleavage furrow through its PH domain. …
- NAID 120005293580
Related Pictures
★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
[★]
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
[★]
- 英
- PH domain
- 関
- プレクストリン相同ドメイン
[★]
- 関
- area、realm、region、regional、segregation、territory、universe
[★]
[★]
肺高血圧症 pulmonary hypertension
[★]
水素イオン指数
[★]
- 関
- See also specific type