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Ubiquitin fusion degradation 1 like

Ufd1, UFD1L, Ufd1p
The protein encoded by this gene forms a complex with two other proteins, nuclear protein localization-4 and valosin-containing protein, and this complex is necessary for the degradation of ubiquitinated proteins. In addition, this complex controls the disassembly of the mitotic spindle and the formation of a closed nuclear envelope after mitosis. Mutations in this gene have been associated with Catch 22 syndrome as well as cardiac and craniofacial defects. Alternative splicing results in multiple transcript variants encoding different isoforms. A related pseudogene has been identified on chromosome 18. [provided by RefSeq, Jun 2009] (from NCBI)
Top mentioned proteins: Ubiquitin, ATPase, p97, CAN, Brachyury
Papers on Ufd1
Characterization of an Additional Binding Surface on the p97 N-Terminal Domain Involved in Bipartite Cofactor Interactions.
Schindelin et al., Würzburg, Germany. In Structure, Feb 2016
This finding explains how cofactors like UFD1/NPL4 and p47 can utilize a bipartite binding mechanism to interact simultaneously with the same p97 monomer via their ubiquitin-like domain and SHP motif.
MALDI-TOF-MS Assay to Detect the Hemizygous 22q11.2 Deletion in DNA from Dried Blood Spots.
Vogt et al., Atlanta, United States. In Clin Chem, Jan 2016
We developed a MALDI-TOF-MS assay that uses DBS to measure the hemizygous deletion of UFD1L, located within the 22q11.2
Mitochondrial Citrate Transporter-dependent Metabolic Signature in the 22q11.2 Deletion Syndrome.
Giulivi et al., Davis, United States. In J Biol Chem, Oct 2015
Nine of ∼30 genes involved in 22qDS have the potential of disrupting mitochondrial metabolism (COMT, UFD1L, DGCR8, MRPL40, PRODH, SLC25A1, TXNRD2, T10, and ZDHHC8).
Gene expression analysis in blood of ultra-high risk subjects compared to first-episode of psychosis patients and controls.
Belangero et al., São Paulo, Brazil. In World J Biol Psychiatry, Jul 2015
RESULTS: We found that UFD1L (ubiquitin fusion degradation 1 like (yeast)) gene was upregulated in UHR group compared to HC and FEP (P = 3.44 × 10(-6) ; P = 9.41 × 10(-6)).
ESCRT-III controls nuclear envelope reformation.
Carlton et al., Bristol, United Kingdom. In Nature, Jul 2015
Localization also requires the p97 complex member ubiquitin fusion and degradation 1 (UFD1).
Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly.
Carra et al., Reggio nell'Emilia, Italy. In Cell Death Differ, 2014
Silencing the VCP co-factors UFD1L and PLAA, which degrade defective ribosomal products (DRIPs) and 60S ribosomes, also impaired SG assembly.
Single site suppressors of a fission yeast temperature-sensitive mutant in cdc48 identified by whole genome sequencing.
Hartmann-Petersen et al., Copenhagen, Denmark. In Plos One, 2014
The last suppressor was an extragenic frame shift mutation in the ufd1 gene, which encodes a known Cdc48 co-factor.
The AAA-ATPase molecular chaperone Cdc48/p97 disassembles sumoylated centromeres, decondenses heterochromatin, and activates ribosomal RNA genes.
Tamaru et al., Vienna, Austria. In Proc Natl Acad Sci U S A, 2014
We demonstrate that CDC48A physically associates with its heterodimeric cofactor UFD1-NPL4, known to bind ubiquitin and SUMO, as well as with SUMO1-modified CenH3 and mutations in NPL4 phenocopy cdc48a mutations.
Chromosome 22q11.2 deletion syndrome: prenatal diagnosis, array comparative genomic hybridization characterization using uncultured amniocytes and literature review.
Wang et al., Taipei, Taiwan. In Gene, 2013
We discuss the genotype-phenotype correlation and the consequence of haploinsufficiency of TBX1, COMT, UFD1L, GNB1L and MED15 in the deleted region.
The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks.
Ramadan et al., Zürich, Switzerland. In Nat Cell Biol, 2011
p97 is recruited to DNA lesions by its ubiquitin adaptor UFD1-NPL4 and Lys-48-linked ubiquitin (K48-Ub) chains, whose formation is regulated by RNF8.
Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.
Ronai et al., Los Angeles, United States. In Proc Natl Acad Sci U S A, 2011
Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control
Cdc48/p97-Ufd1-Npl4 antagonizes Aurora B during chromosome segregation in HeLa cells.
Meyer et al., Essen, Germany. In J Cell Sci, 2011
Data establish Cdc48/p97-Ufd1-Npl4 as a crucial negative regulator of Aurora B early in mitosis of human somatic cells and suggest that the activity of Aurora B on chromosomes needs to be restrained to ensure faithful chromosome segregation.
The UFD1L rs5992403 polymorphism is associated with age at onset of schizophrenia.
Smith et al., In J Psychiatr Res, 2010
This study suggested that AA genotype of UFD1L gene, which is involved in neurodevelopmental processes, may contribute to early-onset schizophrenia. Therefore, rs5992403 polymorphism may not be a risk factor for schizophrenia.
The p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.
Ye et al., Bethesda, United States. In J Biol Chem, 2010
Data suggest that the human cytomegalovirus dislocation reaction in US2 cells is independent of the p97 cofactor Ufd1-Npl4, and different retrotranslocation mechanisms can employ distinct p97 ATPase complexes to dislocate substrates.
Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective cdc48-ufd1-npl4 complex by upregulating cdc48.
Rabinovich et al., Tel Aviv-Yafo, Israel. In Genetics, 2010
Ssz1 restores endoplasmic reticulum-associated protein degradation in cells expressing defective cdc48-ufd1-npl4 complex by upregulating cdc48.
ER-associated degradation of membrane proteins in yeast.
Ghislain et al., Louvain-la-Neuve, Belgium. In Scientificworldjournal, 2005
Delivery of non-native ER proteins to the proteasome requires retrograde transport across the ER membrane and depends on a protein-unfolding machine consisting of Cdc48p, Ufd1p, and Npl4p.
Endoplasmic reticulum-associated protein degradation.
Sommer et al., Berlin, Germany. In Int Rev Cytol, 2002
Moreover, polyubiquitination of ERAD substrates at the ER membrane as well as the cytoplasmic Cdc48p/Npl4p/Ufd1p complex were shown to contribute to this export reaction.
Protein dislocation from the endoplasmic reticulum--pulling out the suspect.
Sommer et al., Berlin, Germany. In Traffic, 2002
Of special interest is the cytoplasmic Cdc48p/Npl4p/Ufd1p complex, which is required for the degradation of various endoplasmic reticulum-associated protein degradation substrates and seems to function in a step after polyubiquitination but before proteasomal digestion.
Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone.
Jentsch et al., Martinsried, Germany. In Cell, 2001
Subsequently, p90 is liberated from its partner for nuclear targeting by the activity of the chaperone-like CDC48(UFD1/NPL4) complex.
A molecular pathway revealing a genetic basis for human cardiac and craniofacial defects.
Srivastava et al., Dallas, United States. In Science, 1999
A screen for mouse genes dependent on dHAND, a transcription factor implicated in neural crest development, identified Ufd1, which maps to human 22q11 and encodes a protein involved in degradation of ubiquitinated proteins.
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