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O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1
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scholarly article
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title
O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1
(English)
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main subject
proteolysis
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based on heuristic
inferred from title
author
Winship Herr
object named as
Winship Herr
series ordinal
9
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Joan W. Conaway
object named as
Joan W Conaway
series ordinal
7
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author name string
Francesca Capotosti
series ordinal
1
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Sophie Guernier
series ordinal
2
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Fabienne Lammers
series ordinal
3
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Patrice Waridel
series ordinal
4
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Yong Cai
series ordinal
5
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Jingji Jin
series ordinal
6
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Ronald C Conaway
series ordinal
8
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language of work or name
English
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publication date
4 February 2011
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published in
Cell
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volume
144
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issue
3
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page(s)
376-88
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cites work
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Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily
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The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein
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O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress
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Control of alpha-herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities
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A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1.
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O-GlcNAc cycling: emerging roles in development and epigenetics
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Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene
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Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase
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O-GlcNAc turns twenty: functional implications for post-translational modification of nuclear and cytosolic proteins with a sugar
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Recruitment of O-GlcNAc transferase to promoters by corepressor mSin3A: coupling protein O-GlcNAcylation to transcriptional repression
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Structural insights into mechanism and specificity of O-GlcNAc transferase
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E2F1 mediates DNA damage and apoptosis through HCF-1 and the MLL family of histone methyltransferases
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Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins
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Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
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The superhelical TPR-repeat domain of O-linked GlcNAc transferase exhibits structural similarities to importin alpha
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Protein kinase inhibition of clinically important staurosporine analogues
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Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors
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Autocatalytic proteolysis of the transcription factor-coactivator C1 (HCF): a potential role for proteolytic regulation of coactivator function
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An activation domain in the C-terminal subunit of HCF-1 is important for transactivation by VP16 and LZIP.
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The cellular C1 factor of the herpes simplex virus enhancer complex is a family of polypeptides
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Regulation of a cytosolic and nuclear O-GlcNAc transferase. Role of the tetratricopeptide repeats
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Functional expression of O-linked GlcNAc transferase. Domain structure and substrate specificity
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Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex
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The THAP-zinc finger protein THAP1 associates with coactivator HCF-1 and O-GlcNAc transferase: a link between DYT6 and DYT3 dystonias
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O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits
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reference URL
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Proteolytic processing is necessary to separate and ensure proper cell growth and cytokinesis functions of HCF-1
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Recombinant O-GlcNAc transferase isoforms: identification of O-GlcNAcase, yes tyrosine kinase, and tau as isoform-specific substrates
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Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
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7 January 2021
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A single-point mutation in HCF causes temperature-sensitive cell-cycle arrest and disrupts VP16 function.
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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7 January 2021
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inferred from DOI database lookup
Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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7 January 2021
based on heuristic
inferred from DOI database lookup
The HCF repeat is an unusual proteolytic cleavage signal
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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WebLogo: A Sequence Logo Generator
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inferred from DOI database lookup
Glycosylation of nucleocytoplasmic proteins: signal transduction and O-GlcNAc
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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7 January 2021
based on heuristic
inferred from DOI database lookup
Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates cytokinesis
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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7 January 2021
based on heuristic
inferred from DOI database lookup
Species selectivity of mixed-lineage leukemia/trithorax and HCF proteolytic maturation pathways
1 reference
stated in
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reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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inferred from DOI database lookup
Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1
1 reference
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reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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HCF-1 amino- and carboxy-terminal subunit association through two separate sets of interaction modules: involvement of fibronectin type 3 repeats
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FJ.CELL.2010.12.030
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inferred from DOI database lookup
Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method
1 reference
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Identifiers
DOI
10.1016/J.CELL.2010.12.030
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4768996
Fatcat ID
release_qe6awznmd5dnfoaax747xxaxe4
0 references
OpenCitations bibliographic resource ID
4768996
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4768996
PubMed publication ID
21295698
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4768996
ResearchGate publication ID
49812022
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