GIT1 (Ab-383) Antibody
- Known as:
- GIT1 (Antibody-383) Antibody
- Catalog number:
- 21707
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- GIT1 (Ab-383) Antibody
Related genes to: GIT1 (Ab-383) Antibody
- Gene:
- GIT1 NIH gene
- Name:
- GIT ArfGAP 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 17q11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2000-07-31
- Date modifiied:
- 2016-10-05
Related products to: GIT1 (Ab-383) Antibody
Related articles to: GIT1 (Ab-383) Antibody
- The optimal growth temperature (OGT) of organisms is valuable in bioprospecting enzymes that work under extreme conditions. Existing OGT prediction models achieve high accuracy but mainly capture trends of overrepresented groups in the training set including organisms that thrive at moderate temperatures and those from well-described taxa. In this study, we incorporated weighted scoring and phylogenetic splits to improve the generalizability of the prediction models. We first built a new growth temperature data set comprising more than 15,000 species distributed over all three domains of life, with special attention to include OGT and extreme temperature data. We then trained machine learning models on the prokaryotic OGT data using proteome-averaged amino acid descriptors. The best-performing model was the multilayer perceptron (MLP) with a test RMSE of 5.49 °C and an of 0.84. The most important proteome features were related to backbone flexibility and charged residues, as well as surface accessibility. The MLP model is integrated in the command line tool OGTFinder and available under MIT license at: https://github.com/SC-Git1/OGTFinder. - Source: PubMed
Publication date: 2026/04/13
Colette SophieFrançois JaldertDe Moor Bartvan Noort Vera - Glycerophosphocholine (GPC) and glycerophosphoinositol (GPI) are phospholipid metabolites generated by phospholipase-mediated deacylation. In budding yeast, they enter cells via the Git1 permease; in fission yeast, the homolog is Tgp1. This study investigates why GPC is toxic to mutants, where Tgp1 is upregulated due to loss of Asp1 pyrophosphatase, resulting in elevated inositol pyrophosphate 1,5-IP. We show that Tgp1 specifically transports GPC, explaining why GPC, but not GPI, impairs growth. Increased GPC uptake slows doubling time but does not reduce viability. Toxicity is relieved by deletion of Gde1, a phosphodiesterase that hydrolyzes GPC to choline and glycerol-3-phosphate. Mutations in either the Gde1 active site or SPX domain also suppress toxicity, and radiolabeling confirms both domains are required for enzymatic activity. GPC is toxic in cells vastly overexpressing Tgp1 even without elevated IP, but Gde1 loss does not suppress this effect. Similarly, in overexpressing the Git3 transporter, GPC provision causes toxicity independent of Gde1. Loss of Gpc1, the acyltransferase converting GPC to lysophosphatidylcholine, does not alter toxicity in either yeast. These findings highlight a conserved process by which GPC regulates growth and reveal a role for IP in modulating this process. - Source: PubMed
Publication date: 2026/02/16
Hrach Victoria LeeSchwer BeateVitek LaneBorowicz MichaelInnokentev AlekseiSanchez Ana MSinger Justin RShuman StewartPatton-Vogt Jana - ARF GTPase protein 1 (GIT1) is a scaffold protein that is overexpressed in hepatocellular carcinoma (HCC) and colorectal cancer (CRC). GIT1 forms a complex with methionine adenosyltransferase 2B (MAT2B) that activates RAS-RAF-MEK-ERK signaling in HCC and CRC to enhance tumorigenicity. Here, we investigated in a proof-of-concept study whether a small molecule that disrupts GIT1-MAT2B interaction can be effective in HCC and CRC treatment. Since the GIT1 crystal structure is unavailable, we developed a molecular model and used computer-based drug discovery approach to screen for small molecules targeting the GIT1 ankyrin repeat domain, the region closest to where MAT2B interacts that is accessible. Of nine compounds tested, compound 3 (C3) selectively interacts with GIT1 and shows an anti-cancer effect in a GIT1-dependent manner. C3 is antiproliferative, induced apoptosis and G2/M cell cycle arrest while inhibiting colony formation and migration in liver and colon cancer cells. C3 lowered interaction between GIT1 and MAT2B, and with downstream effectors cRAF, MEK and ERK, lowering MEK activity and cyclin D1 expression. Unexpectedly, C3 stabilized GIT1 interaction with cyclin B1 while weakening cyclin B1's interaction with components of the anaphase promoting complex, concomitant with sustained cyclin B1 expression and mitosis arrest. In mice, C3 administration was well tolerated and inhibited murine CRC growth and liver metastasis in immune competent mice and human CRC growth in the livers of nude mice. In conclusion, a small molecule inhibitor that disrupts GIT1's normal interactome is a promising new approach to treating liver and colon cancers. - Source: PubMed
Publication date: 2026/02/20
Peng HuiChhimwal JyotiFan WeiWang JiaohongBarbier-Torres LucíaSinha SonalChatterjee AvradipZhang YiTomasi Maria LaudaMato José MMurali RamachandranLu Shelly C - Tip growth is closely tied to fungal pathogenicity. Budding yeast Spa2 (the homolog of GIT1 and GIT2 in mammals), a multi-domain protein and member of the polarisome, orchestrates tip growth in yeasts and other fungi. We identified a conserved short linear motif in the Rab GTPase-activating proteins (RabGAPs) Msb3 and Msb4, and the MAP kinase kinases Ste7 and Mkk1, which mediates their interaction with Spa2. AlphaFold predictions suggest that these initially unstructured motifs adopt an α-helical conformation upon binding to the hydrophobic cleft in the N-terminal domain of Spa2. Altering the predicted key contact residues in either Spa2 or the motif reduces complex stability. Such mutations also cause mis-localization of Msb3, Msb4 and Ste7 within the cell. Deleting the motif in Msb3 or Msb4 abolishes tip-directed growth of the yeast bud. Protein assemblies that spatially confine secretion to specific membrane regions are a common feature of eukaryotic cells. Accordingly, complexes between proteins with this motif and Spa2 were predicted in orthologs and paralogs across selected Opisthokonta, including pathogenic fungi and humans. A search for functional motifs in conformationally flexible regions of all yeast proteins identified Dse3 as a novel Spa2-binding partner. - Source: PubMed
Publication date: 2026/01/13
Bareis LaraSiewert AnnikaGrupp BenjaminBergner TimRead ClarissaTimmermann SteffiSchmid NicoleJohnsson Nils - Integrin adhesion complexes (IACs) are a network of many proteins that serve as anchors of the cell to the extracellular matrix (ECM). In muscle, IACs located at costameres, also serve to transmit the force of muscle contraction to the outside of the cell. We have reported that IACs, which are found at the bases of dense bodies and M-lines, and at muscle cell boundaries (MCB) in muscle, require the RacGEF PIX-1 for their proper assembly or maintenance. We have reported that a RacGAP for the PIX pathway is RRC-1, is in a complex with PIX-1, and that RRC-1 is required for assembly or maintenance of IACs at MCBs. Our previous studies suggested that RRC-1 might be associated with the muscle cell membrane, and here we present evidence that this occurs via its PX domain, a domain that is known to bind to membrane phosphoinositides (PIPs). We predict the existence of a PX domain based on bioinformatic analysis and AlphaFold3, which includes conserved residues characteristic of most PX domains and a PIP binding site. This region of RRC-1 binds to phosphoinositides in vitro. Analysis of a nematode strain that has an in-frame deletion of the PX domain, indicates that normal localization of RRC-1 to the MCB requires both its PX domain and the PIX scaffold protein GIT-1. Lastly, we show that the overexpression of the full length RRC-1, but not RRC-1 with an in-frame deletion of its PX domain, results in reduced accumulation of IAC components and reduced whole animal movement. Our study highlights the importance of RRC-1's lipid interactions at the cell membrane for proper assembly and function of IACs in muscle. - Source: PubMed
Publication date: 2025/12/15
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