Leigh Ann Higa

ORCID: 0000-0003-0117-0397
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About
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Research Areas
  • Ubiquitin and proteasome pathways
  • DNA Repair Mechanisms
  • Cancer-related Molecular Pathways
  • Microtubule and mitosis dynamics
  • Cancer-related gene regulation
  • Epigenetics and DNA Methylation
  • Adipose Tissue and Metabolism
  • 14-3-3 protein interactions
  • Vascular Anomalies and Treatments
  • Genomics and Chromatin Dynamics
  • Zebrafish Biomedical Research Applications
  • Autism Spectrum Disorder Research
  • Tracheal and airway disorders
  • Sharing Economy and Platforms
  • Mitochondrial Function and Pathology
  • Autophagy in Disease and Therapy

Children's Hospital of Philadelphia
2017

University of Utah
2015

Yale University
2002-2007

The CUL4 (cullin 4) proteins are the core components of a new class ubiquitin E3 ligases that regulate cell cycle, DNA replication and damage response. To determine composition ligase complex, we used anti-CUL4 antibody affinity chromatography to isolate associated with human complexes identified them by mass-spectrometry. A novel conserved WD40 domain-containing protein, homologue Drosophila lethal(2) denticleless protein (L2DTL) or fission yeast CDT2, was found associate DDB1. L2DTL also...

10.4161/cc.5.15.3149 article EN Cell Cycle 2006-07-06

Alteration of the control DNA replication and mitosis is considered to be a major cause genome instability. To investigate mechanism that controls stability, we used RNA silencing-interference technique (RNAi) eliminate Drosophila geminin homologue from Schneider D2 (SD2) cells. Silencing by RNAi in SD2 cells leads cessation asynchronous overreplication genome, with containing single giant nuclei partial ploidy between 4N 8N content. The effect deficiency completely suppressed cosilencing...

10.1128/mcb.22.6.1868-1880.2002 article EN Molecular and Cellular Biology 2002-03-01

AbstractThe CUL4-ROC1 E3 ligase complex regulates genome stability, replication, and cell cycle progression. A novel WD40 domain-containing protein, L2DTL, PCNA were identified as proteins associated with CUL4/DDB1 complexes. Inactivation of CUL4A, PCNA, DDB1, or ROC1 induced p53 stabilization growth arrest. DDB1/CUL4A complexes found to physically interact tumor suppressor its regulator MDM2/HDM2. The isolated CUL4A display potent robust polyubiquitination activity towards this is dependent...

10.4161/cc.5.15.3150 article EN cc-by-nc Cell Cycle 2006-07-06

Recent investigation of Cullin 4 (CUL4) has ushered this class multiprotein ubiquitin E3 ligases to center stage as critical regulators diverse processes including cell cycle regulation, developmental patterning, DNA replication, damage and repair, epigenetic control gene expression. CUL4 associates with Damage Binding protein 1 (DDB1) assemble an ligase that targets substrates for ubiquitin-dependent proteolysis. activity is also regulated by the covalent attachment ubiquitin-like NEDD8...

10.1186/1747-1028-2-5 article EN cc-by Cell Division 2007-01-01

The CUL4 (cullin 4) proteins are the core components of a new class ubiquitinE3 ligases that regulate replication and transcription. To examine roles incell cycle regulation, we analyzed effect inactivation in both Drosophilaand human cells. We found loss Drosophila cells causes G1 cell cyclearrest an increased protein level CDK inhibitor Dacapo. Co-elimination ofDacapo with abolishes arrest. In cells, CUL4Ainduces p27Kip1 stabilization arrest which is dependenton presence p27, suggesting...

10.4161/cc.5.1.2266 article EN Cell Cycle 2005-11-22
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