KRIT1 _ CCM1
- Known as:
- KRIT1 _ CCM1
- Catalog number:
- Y213616
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- KRIT1 _ CCM1
Related genes to: KRIT1 _ CCM1
- Gene:
- KRIT1 NIH gene
- Name:
- KRIT1 ankyrin repeat containing
- Previous symbol:
- CCM1
- Synonyms:
- CAM
- Chromosome:
- 7q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-06-02
- Date modifiied:
- 2019-04-23
Related products to: KRIT1 _ CCM1
Anti- KRIT1 CCM1 Antibodyanti-KRIT1anti-KRIT1anti-KRIT1 (1D8)anti-KRIT1 (2C7)anti-KRIT1 (1D8)anti-KRIT1 (1D8) type: Primary antibodies host: Mouseanti-KRIT1 type: Primary antibodies host: MouseBovine Krev interaction trapped protein 1(KRIT1) ELISA kitBovine Krev interaction trapped protein 1(KRIT1) ELISA kit SpeciesBovineBovine KRIT1, ankyrin repeat containing (KRIT1) ELISA kit, Species Bovine, Sample Type serum, plasmaCalmodulin, striated muscle,CCM1,Chicken,Gallus gallusCCM-1 , Host: E. coli, Species: Human, Synonyms: CCM-1; Cerebral cavernous malformations protein 1; KRIT1; KRIT1, ankyrin repeat containing; CAMCCM-1 Anti-Human Host: Rabbit CCM-1; Cerebral cavernous malformations protein 1; KRIT1; KRIT1, ankyrin repeat containing; CAMCCM-1 Anti-Human Host: Rabbit CCM-1; Cerebral cavernous malformations protein 1; KRIT1; KRIT1, ankyrin repeat containing; CAM Related articles to: KRIT1 _ CCM1
- KRIT1 plays a key role in regulating the barrier function of endothelial cells, where it localizes to the adherens junctions, cytoplasm, and nucleus. However, how subcellular localization may regulate KRIT1 remains unclear. Here, we investigate what effect nuclear localization has on its ability to stabilize the endothelial barrier. We generated a KRIT1 mutant lacking the endogenous nuclear localization signal (NLS) and a nuclear-targeted KRIT1 isoform created by attaching the NLS of simian virus 40 and expressed these constructs in cells depleted of endogenous KRIT1. After confirming the relative non-nuclear (KRIT1) and nuclear (KRIT1) enrichment of these constructs using confocal microscopy and cellular fractionation, we assessed whether these constructs were able to functionally rescue phenotypes characteristic of KRIT1-depleted cells. Our results showed that nuclear localized KRIT1 remains fully functional. However, the KRIT1 construct failed to rescue the KRIT1 depletion phenotype. KRIT1 also disrupted binding to ICAP1α, as shown by co-immunoprecipitation. To determine whether the loss of function was due to loss of ICAP1α-mediated conformational change or altered localization, we incorporated two mutants known to disrupt the N- to C-terminal interaction in KRIT1, NPXY → APAA or W688A into our KRIT1 and KRIT1 constructs. The presence of these additional mutations had unexpected effects on nuclear localization of KRIT1 and KRIT1 but were able to restore barrier-stabilizing function to KRIT1. Overall, our findings provide key insights into the role of ICAP1α binding and nuclear localization in the regulation of KRIT1 and raise new questions regarding potentially novel functions of KRIT1 in the nucleus. - Source: PubMed
Publication date: 2026/05/10
Perrelli AndreaGlading Angela J - Cerebral cavernous malformations (CCM) are angiographically occult vascular anomalies of the brain, characterized by dilated capillaries, increased vascular permeability, and loss of endothelial junctional protein complexes. Loss-of-function mutations in one of the three genes, namely KRIT1/CCM1, CCM2, and PDCD10/CCM3, have been associated with the disease pathogenesis, although the contribution of other genetic determinants besides CCM genes has been recently identified. Despite recent advances in understanding the molecular mechanism of the disease, the current lack of therapies and its unpredictable clinical behavior represent a significant challenge in the identification of diagnostic biomarkers. ADGRL4/ETLD1 (epidermal growth factor, latrophilin and seven transmembrane domain-containing protein 1), a G-protein coupled receptor (GPCR) protein is a known biomarker of angiogenesis and inflammation, and it has been suggested to be a key therapeutic target for stroke and high-grade gliomas. However, the relevance of ELTD1 in CCM pathogenesis remains unexplored. - Source: PubMed
Publication date: 2026/05/08
Perrelli AndreaAhmed AshraqatOnisiforou AnnaBoulday GwenolaZalvide JuanPombo Celia MMartínez José EPaolini AlessioAbdelilah-Seyfried SalimPetrakakis IoannisKunz Wolfram SGeffers RobertHartmann ChristianBini WalterBaltsavias GerasimosSamii AmirBertalanffy HelmutRetta Saverio FGlading Angela JKar Souvik - K-Rev Interaction Trapped protein-1 (KRIT1) is a scaffold protein that forms functional protein complexes involved in physiologically important signaling networks. While it is primarily recognized for its association with Cerebral Cavernous Malformations (CCMs), KRIT1 may also play critical roles in tumor formation and the acquisition of malignant phenotypes, regulating cell adhesion, cytoskeletal dynamics, and angiogenesis. In this study, we investigated the role of KRIT1 in cancer cell migration and metastasis, with a focus on identifying novel interacting proteins and characterizing the intracellular signaling pathways activated upon its loss. By using a yeast two-hybrid screening, we identified Kinesin Family Member 1C (KIF1C), a protein involved in regulating podosome and invadopodium elongation, as a novel binding partner of KRIT1, and the interaction was confirmed in melanoma and epithelial cancer cells. In silico docking and interaction interface analyses supported the KRIT1-KIF1C interaction, providing structural insight into the binding mode as shown experimentally. We also found that SRC and focal adhesion kinase (FAK) phosphorylation, as well as Ras homolog family member A (RhoA) expression, represent additional pathways affected by the loss of KRIT1. This study confirms our earlier hypothesis that KRIT1 functions as a tumor suppressor and uncovers a compelling link between its loss and enhanced cancer aggressiveness. - Source: PubMed
Publication date: 2026/04/10
Paradisi LucreziaGuazzi PaoloMacis MatteoFinetti FrancescaTrezza AlfonsoDe Paolo RaffaellaRoncetti MartaMarshall John FPoliseno LauraFinetti FedericaTrabalzini Lorenza - Cerebral cavernous malformations (CCMs) are vascular lesions characterized by a collection of thin-walled capillaries with slow blood flow, which are often identified incidentally on MRI. CCMs are the most common cerebral vascular malformation after developmental venous anomalies. Familial CCM (FCCM) is a rare autosomal dominant disorder characterized by several lesions throughout the central nervous system. We report the case of a 47-year-old female patient who presented to the neurology clinic with a chief complaint of transient dysphagia. An MRI of the brain without contrast, including susceptibility-weighted imaging (SWI), demonstrated numerous punctate foci of susceptibility-related signal loss throughout the cerebral and cerebellar hemispheres. Genetic testing revealed a pathogenic KRIT1 mutation, confirming FCCM. The patient's dysphagia resolved within one month of the initial onset and, fortunately, has not returned. This case highlights an atypical presentation of FCCM and the importance of an extensive workup in patients with unexplained neurologic symptoms. - Source: PubMed
Publication date: 2026/02/05
Scott Madison LRoss Daniel E - Regulated expression of Kruppel like factor (KLF) transcription factors is essential for normal maintenance of endothelial cells, but loss of either K-Rev interaction trapped 1 (KRIT1) or cerebral cavernous malformations 2 (CCM2) proteins results in significant over-expression of KLF4 protein, causing the cerebrovascular disorder, cerebral cavernous malformations. Here, combining knockdown and reconstitution in an endothelial cell line, with co-immunoprecipitation, biophysical analysis of purified proteins, and co-crystallography, we find that to restrain KLF4 expression, two CCM2 proteins must cluster on a single KRIT1, with the PTB domain of each CCM2 protein binding either the second or third NPxF motif within KRIT1. This clustering of two PTB domains to a single peptide reveals a previously unobserved mechanism for PTB domain recruitment to partner proteins. Overall, our data support a model where clustering of two CCM2 molecules to one KRIT1 is required for normal regulation of expression of KLF4 transcription factor. - Source: PubMed
Publication date: 2026/02/13
Huet-Calderwood ClotildeFisher Oriana SDas SreyaSu Valerie LBoggon Titus JCalderwood David A