ArticleOncogene2006
CRIPak, a novel endogenous Pak1 inhibitor.
Article in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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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.
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Who cites it
24 citing papers in PubMed, 46 citations in OpenAlex.
- Article
- Modulating PAK1: Accessory Proteins as Promising Therapeutic Targets.Biomolecules · 2025Review
- Genome-Wide Association Study Identifies Genetic Variants Associated with Rotator Cuff Tear-A Pilot Study.Diagnostics (Basel, Switzerland) · 2022Article
- Breast Ultrasound Microvascular Imaging and Radiogenomics.Korean journal of radiology · 2021Review
- Gene Expression and RNA Splicing Imputation Identifies Novel Candidate Genes Associated with Osteoporosis.The Journal of clinical endocrinology and metabolism · 2020Article
- p21-Activated Kinases in Thyroid Cancer.Endocrinology · 2020Review
- Germline Sequencing Identifies Rare Variants in Finnish Subjects with Familial Germ Cell Tumors.The application of clinical genetics · 2020Article
- Landscape of transcriptomic interactions between breast cancer and its microenvironment.Nature communications · 2019Article
- Genome-wide analysis of genetic predisposition to Alzheimer's disease and related sex disparities.Alzheimer's research & therapy · 2019Article
- Loose ends: almost one in five human genes still have unresolved coding status.Nucleic acids research · 2018Article
- Genomic profile of human meningioma cell lines.PloS one · 2017Article
- Cancer as the Disintegration of Robustness: Population-Level Variance in Gene Expression Identifies Key Differences Between Tobacco- and HPV-Associated Oropharyngeal Carcinogenesis.Archives of pathology & laboratory medicine · 2015Article
- Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion.Advances in experimental medicine and biology · 2015Review
- Cis and trans effects of human genomic variants on gene expression.PLoS genetics · 2014Article
- Molecular pathways: targeting p21-activated kinase 1 signaling in cancer--opportunities, challenges, and limitations.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012Review
- PAK family kinases: Physiological roles and regulation.Cellular logistics · 2012Article
- RAC3 is a pro-migratory co-activator of ERα.Oncogene · 2011Article
- Loss of Rho GDIα and resistance to tamoxifen via effects on estrogen receptor α.Journal of the National Cancer Institute · 2011Article
- Frequent loss of genome gap region in 4p16.3 subtelomere in early-onset type 2 diabetes mellitus.Experimental diabetes research · 2011Article
- PAK1 as a therapeutic target.Expert opinion on therapeutic targets · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
p21-activated protein kinase 1 (Pak1) plays an important role in several cellular processes, including cytoskeleton reorganization, promotion of the cell survival, and the estrogen receptor (ER) signaling. Pak1 expression and activity is deregulated in a number of cancers. Pak1 is activated by a variety of physiological signals; however, less is known about the negative regulators of Pak1. Here, we report a negative regulator of Pak1. By performing a yeast two-hybrid screen of a mammary gland library, we identified cysteine-rich inhibitor of Pak1 (CRIPak) as a novel Pak1-interacting protein. We found that CRIPak is an intronless gene that localized to chromosome 4p16.3. It contains 13 zinc-finger domains and has three trypsin inhibitor-like, cysteine-rich domains and is widely expressed in a number of human cells and tissues. We further found that CRIPak interacted with Pak1 through the N-terminal regulatory domain and inhibited Pak1 kinase in both in vitro and in vivo assays. CRIPak inhibited Pak1-mediated LIM kinase activation and enhancement of ER transactivation. Conversely, selective inhibition of the endogenous CRIPak resulted in an increased Pak1 activity, and consequently, increased cytoskeleton remodeling and Pak1-mediated ER transactivation activity. The hormonal stimulation of cells enhanced CRIPak expression and promoted its colocalization with ER in the nuclear compartment. Our findings suggest that CRIPak is a novel negative regulator of the Pak1 and has a role in the modulation of Pak1-mediated ER transactivation in breast cancer cells.
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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.