ArticleThe Journal of biological chemistry2012
Molecular basis for the association of microcephalin (MCPH1) protein with the cell division cycle protein 27 (Cdc27) subunit of the anaphase-promoting complex.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Genetic polymorphisms of theFrontiers in genetics · 2026Article
- Altered neuroepithelial morphogenesis and migration defects in iPSC-derived cerebral organoids and 2D neural stem cells in familial bipolar disorder.Oxford open neuroscience · 2024Article
- Evaluation of DNA repair capacity in parents of pediatric patients diagnosed with autism spectrum disorder using the comet assay procedure.IBRO neuroscience reports · 2023Article
- Genetic Primary Microcephalies: When Centrosome Dysfunction Dictates Brain and Body Size.Cells · 2023Review
- Multifaceted Microcephaly-Related Gene MCPH1.Cells · 2022Review
- Molecular Genetics of Microcephaly Primary Hereditary: An Overview.Brain sciences · 2021Review
- The importance of CDC27 in cancer: molecular pathology and clinical aspects.Cancer cell international · 2021Review
- Mitotic entry upon Topo II catalytic inhibition is controlled by Chk1 and Plk1.The FEBS journal · 2020Article
- The E3 ubiquitin ligase APC/CThe EMBO journal · 2017Article
- Structural Insight into Anaphase Promoting Complex 3 Structure and Docking with a Natural Inhibitory Compound.Advanced biomedical research · 2017Article
- The unconventional kinetoplastid kinetochore: from discovery toward functional understanding.Biochemical Society transactions · 2016Review
- Mcph1/Brit1 deficiency promotes genomic instability and tumor formation in a mouse model.Oncogene · 2015Article
- MiR-27a modulates radiosensitivity of triple-negative breast cancer (TNBC) cells by targeting CDC27.Medical science monitor : international medical journal of experimental and clinical research · 2015Article
- MCPH1: a window into brain development and evolution.Frontiers in cellular neuroscience · 2015Review
- The Drosophila MCPH1-B isoform is a substrate of the APCCdh1 E3 ubiquitin ligase complex.Biology open · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Microcephalin (MCPH1), the first gene identified as causative for primary recessive autosomal microcephaly, is aberrantly expressed in autism-like disorders and human malignancy of breast and ovarian origin. MCPH1, the encoded protein product, has been implicated in various cellular processes including the DNA damage checkpoint, DNA repair, and transcription. Although our understanding of the cellular context in which MCPH1 operates continues to develop, a structural understanding of the C-terminal tandem BRCT domains of MCPH1 remains unexplored. Here, we identify cell division cycle protein 27 (Cdc27), a component of the anaphase-promoting complex (APC/C), as a novel interacting partner of MCPH1. We provide in vitro and in vivo evidence that the C-terminal tandem BRCT domains of MCPH1 (C-BRCTs) bind Cdc27 in a phosphorylation-dependent manner. To characterize this interaction further, we determined the structure of MCPH1 C-BRCTs in complex with a phosphorylated Cdc27 peptide (pCdc27) using x-ray crystallography. Based on this structure, we identified single amino acid mutations targeted at the binding interface that disrupted the MCPH1-pCdc27 interaction. Collectively, our data define the biochemical, structural, and cellular determinants of the novel interaction between MCPH1 and Cdc27 and suggest that this interaction may occur within the larger context of MCPH1-APC/C.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.