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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Zinc finger, DHHC-type containing 17

HIP14, Huntingtin interacting protein 14, ZDHHC17, DHHC17
Top mentioned proteins: huntingtin, SNAP-25, CAN, ACID, Glutamate Decarboxylase
Papers on HIP14
ZDHHC17 promotes axon outgrowth by regulating TrkA-tubulin complex formation.
Hao et al., Jinan, China. In Mol Cell Neurosci, Sep 2015
ZDHHC17 is a member of the DHHC (Asp-His-His-Cys)-containing family, a family of highly homologous proteins.
Aberrant palmitoylation in Huntington disease.
Hayden et al., Vancouver, Canada. In Biochem Soc Trans, Apr 2015
In the presence of the HD mutation, the interactions between huntingtin (HTT) and huntingtin interacting protein 14 (HIP14 or DHHC17) and HIP14-like (DHHC13, a HIP14 orthologue), palmitoyl acyltransferases for HTT, are disturbed, resulting in reduced palmitoylation of HTT.
Huntingtin interacting proteins 14 and 14-like are required for chorioallantoic fusion during early placental development.
Hoodless et al., Vancouver, Canada. In Dev Biol, Feb 2015
HTT is palmitoylated by huntingtin interacting proteins 14 and 14-like (HIP14 and HIP14L or ZDHHC17 and 13 respectively).
Regulation of GABA Neurotransmission by Glutamic Acid Decarboxylase (GAD).
Wu et al., Atlantic City, United States. In Curr Pharm Des, 2014
Specific to GAD65 but not GAD67 is palmitoylation by HIP14 which facilitates GAD65 anchoring to SV and enhances the contribution of vesicular GABA to neurotransmission.
Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).
Coleman et al., Cambridge, United Kingdom. In J Biol Chem, 2014
Furthermore, we identify several zDHHC palmitoyltransferases that influence NMNAT2 palmitoylation and subcellular localization, among which a role for zDHHC17 (HIP14) in neuronal NMNAT2 palmitoylation is best supported by our data.
The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease.
Hayden et al., Vancouver, Canada. In Hum Mol Genet, 2014
HIP14 is the most highly conserved of 23 human palmitoyl acyltransferases (PATs) that catalyze the post-translational addition of palmitate to proteins, including huntingtin (HTT).
Memory and synaptic deficits in Hip14/DHHC17 knockout mice.
Raymond et al., Vancouver, Canada. In Proc Natl Acad Sci U S A, 2014
Here we describe that the constitutive loss of huntingtin interacting protein 14 (Hip14, also known as DHHC17), a single member of the broad palmitoyl acyltransferase (PAT) family, produces marked alterations in synaptic function in varied brain regions and significantly impairs hippocampal memory and synaptic plasticity.
Identification of binding sites in Huntingtin for the Huntingtin Interacting Proteins HIP14 and HIP14L.
Hayden et al., Vancouver, Canada. In Plos One, 2013
Huntingtin Interacting Protein 14 (HIP14) and Huntingtin Interacting Protein 14-like (HIP14L) are palmitoyl acyltransferases (PATs), enzymes that mediate the post-translational addition of long chain fatty acids to proteins in a process called palmitoylation.
Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease.
Davis et al., Detroit, United States. In Chem Biol, 2013
As a first application, we have used ABE/SILAM to look at Huntington's disease (HD), profiling palmitoylation change in two HD-relevant mouse mutants: the transgenic HD model mouse YAC128 and the hypomorphic Hip14-gt mouse, which has sharply reduced expression for HIP14 (Zdhhc17), a palmitoyl-transferase implicated in the HD disease process.
DHHC17 palmitoylates ClipR-59 and modulates ClipR-59 association with the plasma membrane.
Du et al., Boston, United States. In Mol Cell Biol, 2013
We found that, among 23 mammalian DHHC palmitoyltransferases, DHHC17 is the major ClipR-59 palmitoyltransferase, as evidenced by the fact that DHHC17 interacted with ClipR-59 and palmitoylated ClipR-59 at Cys534 and Cys535.
Dysregulated striatal neuronal processing and impaired motor behavior in mice lacking huntingtin interacting protein 14 (HIP14).
Rebec et al., Bloomington, United States. In Plos One, 2012
Huntingtin interacting protein 14 (HIP14) is a PAT that acts on proteins associated with neuronal transmission, suggesting that deficient protein palmitoylation by HIP14, which occurs in the YAC128 model of Huntington's disease (HD), might have deleterious effects on neurobehavioral processing.
Altered Neuronal Dynamics in the Striatum on the Behavior of Huntingtin Interacting Protein 14 (HIP14) Knockout Mice.
Rebec et al., Bloomington, United States. In Brain Sci, 2012
Growing evidence suggests that huntingtin interacting protein 14 (HIP14) contributes to HD neuropathology.
Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases.
Hayden et al., Vancouver, Canada. In Prog Neurobiol, 2012
In total six PATs (HIP14, HIP14L, ZDHHC8, ZDHHC9, ZDHHC12, and ZDHHC15) and one thioesterase (PPT1) have been implicated in Huntington disease (HD), Alzheimer disease, schizophrenia, mental retardation, and infantile and adult onset forms of neuronal ceroid lipofuscinosis.
Low levels of human HIP14 are sufficient to rescue neuropathological, behavioural, and enzymatic defects due to loss of murine HIP14 in Hip14-/- mice.
Hayden et al., Vancouver, Canada. In Plos One, 2011
Low levels of human HIP14 are sufficient to rescue neuropathological, behavioural, and enzymatic defects due to loss of murine HIP14 in Hip14-/- mice.
Altered palmitoylation and neuropathological deficits in mice lacking HIP14.
Hayden et al., Vancouver, Canada. In Hum Mol Genet, 2011
altered palmitoylation mediated by HIP14 may contribute to HD.
Huntingtin-interacting protein 14 is a type 1 diabetes candidate protein regulating insulin secretion and beta-cell apoptosis.
Størling et al., Denmark. In Proc Natl Acad Sci U S A, 2011
Immunohistochemical analysis of pancreatic sections demonstrated that HIP14 is almost exclusively expressed in insulin-positive cells in islets of Langerhans.
Wild-type HTT modulates the enzymatic activity of the neuronal palmitoyl transferase HIP14.
Hayden et al., Vancouver, Canada. In Hum Mol Genet, 2011
Wild-type HTT modulates the enzymatic activity of the neuronal palmitoyl transferase HIP14.
Palmitoyl acyltransferase zD17 mediates neuronal responses in acute ischemic brain injury by regulating JNK activation in a signaling module.
Cynader et al., Vancouver, Canada. In J Neurosci, 2011
Novel peptides have been developed that target the jun N-terminus kinase (JNK)-interacting motif on zD17 to selectively block enhancement of the zD17-Jun N terminus kinase (JNK) interaction and the activation of JNK isoforms 2 and 3.
Insight into renal Mg2+ transporters.
Bindels et al., Nijmegen, Netherlands. In Curr Opin Nephrol Hypertens, 2011
In addition to the well known transient receptor potential channel melastatin (TRPM), members 6 and 7, and the mitochondrial transporter Mrs2, additional Mg-transporting protein families can be acknowledged including the magnesium (Mag) transporters, the solute carrier (SLC) family 41 members, ancient conserved domain proteins (ACDP), nonimprinted in Prader-Willi/Angelman syndrome (NIPA) proteins, membrane Mg transporters (MMgT) and huntingtin-interacting protein 14 (HIP14).
Molecular identification of ancient and modern mammalian magnesium transporters.
Quamme, Vancouver, Canada. In Am J Physiol Cell Physiol, 2010
However, other newly identified mammalian transporters, including TRPM6/7, MagT, NIPA, MMgT, and HIP14 families, are not represented in prokaryotic genomes, suggesting more recent development.
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