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@article{karttunen_oxygen-dependent_2015,

title = {Oxygen-dependent hydroxylation by FIH regulates the TRPV3 ion channel.},

author = {Sarah Karttunen and Michael Duffield and Nathan R Scrimgeour and Lauren Squires and Wai Li Lim and Mark L Dallas and Jason L Scragg and Johana Chicher and Keyur A Dave and Murray L Whitelaw and Chris Peers and Jeffrey J Gorman and Jonathan M Gleadle and Grigori Y Rychkov and Daniel J Peet},

doi = {10.1242/jcs.158451},

issn = {1477-9137 0021-9533},

year  = {2015},

date = {2015-01-01},

journal = {Journal of cell science},

volume = {128},

number = {2},

pages = {225--231},

abstract = {Factor inhibiting HIF (FIH, also known as HIF1AN) is an oxygen-dependent asparaginyl hydroxylase that regulates the hypoxia-inducible factors (HIFs). Several proteins containing ankyrin repeat domains (ARDs) have been characterised as substrates of FIH, although there is little evidence for a functional consequence of hydroxylation on these substrates. This study demonstrates that the transient receptor potential vanilloid 3 (TRPV3) channel is hydroxylated by FIH on asparagine 242 within the cytoplasmic ARD. Hypoxia, FIH inhibitors and mutation of asparagine 242 all potentiated TRPV3-mediated current, without altering TRPV3 protein levels, indicating that oxygen-dependent hydroxylation inhibits TRPV3 activity. This novel mechanism of channel regulation by oxygen-dependent asparaginyl hydroxylation is likely to extend to other ion channels.},

note = {Place: England},

keywords = {alpha Subunit/genetics/*metabolism, Amino Acid Sequence, Ankyrin Repeat/genetics, Cell Hypoxia/*genetics, FIH, HEK293 Cells, Humans, Hydroxylation, Hydroxylation/genetics, Hypoxia, Hypoxia-Inducible Factor 1, Mixed Function Oxygenases/antagonists & inhibitors/genetics/*metabolism, Mutation, Oxygen/metabolism, PPSE, Protein Binding, Repressor Proteins/antagonists & inhibitors/genetics/*metabolism, TRPV Cation Channels/genetics/*metabolism, TRPV3},

pubstate = {published},

tppubtype = {article}

}

@article{wilkins_differences_2009,

title = {Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1).},

author = {Sarah E Wilkins and Jaana Hyvärinen and Johana Chicher and Jeffrey J Gorman and Daniel J Peet and Rebecca L Bilton and Peppi Koivunen},

doi = {10.1016/j.biocel.2009.01.005},

issn = {1878-5875 1357-2725},

year  = {2009},

date = {2009-01-01},

journal = {The international journal of biochemistry & cell biology},

volume = {41},

number = {7},

pages = {1563--1571},

abstract = {FIH-1, factor inhibiting hypoxia-inducible factor-1 (HIF-1), regulates oxygen sensing by hydroxylating an asparagine within HIF-alpha. It also hydroxylates asparagines in many proteins containing ankyrin repeats, including Notch1-3, p105 and I?B?. Relative binding affinity and hydroxylation rate are crucial determinants of substrate selection and modification. We determined the contributions of substrate sequence composition and length and of oxygen concentration to the FIH-1-binding and/or hydroxylation of Notch1-4 and compared them with those for HIF-1alpha. We also demonstrated hydroxylation of two asparagines in Notch2 and 3, corresponding to Sites 1 and 2 of Notch1, by mass spectrometry for the first time. Our data demonstrate that substrate length has a much greater influence on FIH-1-dependent hydroxylation of Notch than of HIF-1alpha, predominantly through binding affinity rather than maximal reaction velocity. The K(m) value of FIH-1 for Notch1, textless 0.2 microM, is at least 250-fold lower than that of 50 microM for HIF-1alpha. Site 1 of Notch1-3 appeared the preferred site of FIH-1 hydroxylation in these substrates. Interestingly, binding of Notch4 to FIH-1 was observed with an affinity almost 10-fold lower than for Notch1-3, but no hydroxylation was detected. Importantly, we demonstrate that the K(m) of FIH-1 for oxygen at the preferred Site 1 of Notch1-3, 10-19 microM, is an order of magnitude lower than that for Site 2 or HIF-1alpha. Hence, at least during in vitro hydroxylation, Notch is likely to become efficiently hydroxylated by FIH-1 even under relatively severe hypoxic conditions, where HIF-1alpha hydroxylation would be reduced.},

note = {Place: Netherlands},

keywords = {alpha Subunit/*metabolism, Amino Acid Sequence, Animals, Asparagine/metabolism, Humans, Hydroxylation, Hypoxia-Inducible Factor 1, Kinetics, Mice, Mixed Function Oxygenases, Molecular Sequence Data, Notch/chemistry/*metabolism, Oxygen/metabolism, Peptides/chemistry/metabolism, PPSE, Protein Binding, Receptors, Recombinant Proteins/metabolism, Repressor Proteins/*metabolism, Substrate Specificity},

pubstate = {published},

tppubtype = {article}

}

@article{meister_conversion_1985,

title = {Conversion of a radiolabelled ecdysone precursor, 2,22,25-trideoxyecdysone, by embryonic and larval tissues of Locusta migratoria},

author = {Marie F Meister and Jean-Luc Dimarcq and Christine Kappler and Charles Hetru and Marie Lagueux and R Lanot and B Luu and Jules A Hoffmann},

issn = {0303-7207},

year  = {1985},

date = {1985-06-01},

journal = {Mol. Cell. Endocrinol.},

volume = {41},

number = {1},

pages = {27--44},

abstract = {A high specific activity tritiated ecdysone precursor, 2,22,25-trideoxyecdysone, was used to probe the capacity of various embryonic and larval tissues to perform the last 3 hydroxylation steps in ecdysone biosynthesis. Embryos at early stages of development, prior to the differentiation of their endocrine glands and embryonic heads, thoraces and abdomens of later stages, were found to have the capacity to hydroxylate the precursor to ecdysone. Larval epidermis and fat body are also able to transform 2,22,25-trideoxyecdysone into ecdysone; Malpighian tubules and midgut hydroxylate the precursor at C-2 but are apparently unable to hydroxylate both at C-22 and C-25. Larval prothoracic glands convert the precursor to ecdysone at a very efficient rate, which is 1-2 magnitudes higher than that of the other tissues investigated; several data argue for the existence of a privileged sequence of hydroxylations, C-25, C-22, C-2, in the larval prothoracic glands.},

keywords = {Abdomen, Animals, Cholestenones, Chromatography, Ecdysone, Epidermis, Fat Body, Grasshoppers, Head, High Pressure Liquid, hoffmann, Hydroxylation, Larva, M3i, Malpighian Tubules, Thorax},

pubstate = {published},

tppubtype = {article}

}

@article{feyereisen_dynamics_1976,

title = {Dynamics of ecdysone metabolism after ingestion and injection in Locusta migratoria},

author = {R Feyereisen and Marie Lagueux and Jules A Hoffmann},

issn = {0016-6480},

year  = {1976},

date = {1976-07-01},

journal = {Gen. Comp. Endocrinol.},

volume = {29},

number = {3},

pages = {319--327},

keywords = {Animals, Ecdysone, Grasshoppers, hoffmann, Hydroxylation, Injections, Intestines, Larva, M3i, Malpighian Tubules, Oral},

pubstate = {published},

tppubtype = {article}

}

@article{hoffmann_molting_1974,

title = {Molting hormone titer and metabolic fate of injected ecdysone during the fifth larval instar and in adults of Locusta migratoria (Orthoptera)},

author = {Jules A Hoffmann and J Koolman and P Karlson and P Joly},

issn = {0016-6480},

year  = {1974},

date = {1974-01-01},

journal = {Gen. Comp. Endocrinol.},

volume = {22},

number = {1},

pages = {90--97},

keywords = {Age Factors, Animals, Chromatography, Ecdysone, Feces, Grasshoppers, hoffmann, Hydroxylation, Invertebrate Hormones, Larva, M3i, Thin Layer, Time Factors, Tritium},

pubstate = {published},

tppubtype = {article}

}