Anti-Mouse MICALL1 (KIAA1668), Rabbit Polyclonal
- Known as:
- Antibody toMouse MICALL1 (KIAA1668), Rabbit Polyclonal
- Catalog number:
- mka1668pa
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Sceti
- Gene target:
- Anti-Mouse MICALL1 (KIAA1668) Rabbit Polyclonal
Related genes to: Anti-Mouse MICALL1 (KIAA1668), Rabbit Polyclonal
- Gene:
- MICALL1 NIH gene
- Name:
- MICAL like 1
- Previous symbol:
- -
- Synonyms:
- MIRAB13, KIAA1668, MICAL-L1
- Chromosome:
- 22q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2006-11-24
- Date modifiied:
- 2015-12-07
Related products to: Anti-Mouse MICALL1 (KIAA1668), Rabbit Polyclonal
Related articles to: Anti-Mouse MICALL1 (KIAA1668), Rabbit Polyclonal
- Rhotekin (RTKN), a Rho GTPase effector, promotes the development of malignancies, including breast, gastric, and colon cancers, by enhancing cell proliferation and migration while inhibiting apoptosis. Despite its oncogenic role, the phosphoregulatory network of RTKN remains largely unexplored, with no experimental evidence on its upstream kinases and functional phosphosites. To characterize RTKN-associated phosphorylation dynamics, PubMed-indexed studies were systematically retrieved using predefined MeSH terms to compile large-scale cellular phosphoproteomics datasets. Analysis of 618 quantitative profiling and 179 differential abundance datasets identified 27 Class-I phosphosites in RTKN. Among these, five sites-Ser106, Ser220, Ser520, Ser529, and Ser543 were consistently observed across multiple datasets, suggesting them as predominant sites with potential functional significance. Structural mapping of predominant sites onto the AlphaFold2-predicted model indicated that these sites are located in accessible regions, highlighting their potential susceptibility to kinase-mediated regulation. As these sites represent understudied phosphosites, a robust strategy was employed to identify their functional role by assessing co-regulated phosphosites on other proteins (PsOPs). ACIN1_Ser243, CTNNA1_Ser641, and SHROOM2_Ser1036 were among the top positively co-regulated PsOPs, whereas MICALL1_Ser644, PRP4K_Ser366, and MYO18A_Ser1970 were negatively co-regulated. PsOPs were mainly involved in apoptosis, cell growth, motility, and cytoskeletal reorganization, suggesting potential functional convergence with RTKN. Additionally, phosphorylation at RTKN Ser520 and Ser543 co-occurred across multiple datasets. Moreover, TRPM7 and PAK4 were identified as predicted upstream kinases phosphorylating RTKN at Ser220 and Ser520. Pathway analysis showed involvement of co-regulated proteins in cancer-associated signaling pathways. These findings provide a foundation for future research to elucidate the phosphosite-specific role of RTKN in cancer. - Source: PubMed
Publication date: 2026/04/10
Palollathil AkhinaMahin AlthafGopalakrishnan Athira PerunellySambreena AlimathUmmar SamseeraShivamurthy Prathik BasthikoppaGanesan RVijayakumar ManavalanRaju Rajesh - The Eps15 Homology Domain protein-1 (EHD1) is an ATPase and key endocytic regulatory protein required for optimal receptor recycling, and primary ciliogenesis. Over the past decade, a central role for EHD1 has been identified in the fission of endosomes. Despite these findings, additional evidence has also pointed at a potential function of EHD1 in the regulation of microtubules. Herein, we demonstrate that EHD1 regulates the distribution of endosomes, and conversely, centrosome depletion alters EHD1 localization in cells. We show that endogenous EHD1 is found in a complex with various endogenous tubulins including TUBB3, TUBB1, α-tubulin and γ-tubulin, interactions that are independent of intact microtubules, and appear to be indirect. Depletion of key individual EHD1 interaction partners that are known to bind tubulin fail to impede EHD1-tubulin interactions, suggesting that either several proteins are capable of mediating EHD1's connection with microtubules, or that the bridging interaction partner remains to be identified. Functionally, EHD1 depletion leads to impaired microtubule regrowth and decreased end-binding protein displacement, suggesting a role for EHD1 in modulating microtubule plus-end dynamics. Finally, EHD1's role in microtubule regulation appears to be evolutionarily conserved, as single-cell stage C. elegans embryos with a dysfunctional EHD1/RME-1 protein displayed enhanced tubulin accumulation at metaphase spindle poles. Our findings strongly support a previously unaddressed role for EHD1 in microtubule regulation. - Source: PubMed
Publication date: 2026/01/27
Ashraf BazellaReddick-Umoja JourneyGrant JasmynIyer JyotiNaslavsky NaavaCaplan Steve - Members of the family of molecule interacting with CASL protein (MICAL) proteins play crucial roles in the cytoskeleton rearrangements by promoting depolymerization of F-actin via oxidation of the specific methionine residues to methionine-sulfoxides. These proteins also have multiple other functions and are related to the pathogenesis of various maladies. However, not much is known about the prevalence and functionality of intrinsically disordered regions in MICALs. To fill this gap, we conducted a comprehensive bioinformatics analysis of five human MICAL protein family members, MICAL1, MICAL2, MICAL3, MICAL-L1, and MICAL-L2, to assess their intrinsic disorder characteristics. We also focused on the top most disordered interactors of these proteins. We utilized a set of bioinformatics tools, FuzDrop, RIDAO, InterPro, IuPred, STRING, AlphaFold, and UniProt, for the extensive analysis of these proteins. This analysis revealed that all five MICALs are highly disordered; they take part in myriad of cellular functions, and are also involved in pathogenesis of various diseases, such as neurodegeneration, cancer, and muscle dystrophy. Our study focused on the intrinsic disorder of these proteins to highlight important implications of disorder in protein functionality. These insights may help to find out potential therapeutic targets in biological processes controlled by MICAL proteins. - Source: PubMed
Publication date: 2025/12/23
Ashraf Hafiza NimraUversky Vladimir N - Most patients with biliary tract cancer (BTC) do not derive durable clinical benefit (DCB) from immune checkpoint inhibitors (ICIs), underscoring the urgent need for predictive biomarkers. While urinary proteomics represents a non-invasive approach for biomarker discovery and mechanism exploration, its utility in ICI-treated patients with cancer remains unexplored. - Source: PubMed
Publication date: 2026/06/09
Wang ShanshanGuo ZhengguangSun BoyuLiu KaiChao JiashuoXun ZiyuWang YunchaoXu ZiboHuang ZiyueWang HaoTan YangZhang NanPiao MingjianZhang LonghaoLi ChengjieLi ShuofengLi JiongyuanSun HaidanQi FengWang AiweiYang XiaoBoZhu ChengpeiWang HanpingSun WeiZhao Haitao - The present study aimed to explore runs of homozygosity (ROH), Heterozygosity Enriched Regions (HER) using the sliding window approach in both PLINK and detectRUNS, as well as the consecutive SNP approach in detectRUNS and their association with important economic traits. Genomic inbreeding coefficient based on ROH and heterosis coefficient based on HER were also estimated among crossbred (n = 81) by using GGP_HDv3_C genotyping assay. Total ROH varied from around 600 in the sliding window approach and almost double in the Consecutive SNP approach of detectRUNS. Similarly, the HER are 756 in the sliding window and 771 in the Consecutive SNP method. The mean inbreeding coefficient range varied in different approaches, i.e., 0.016-0.022 is observed based on ROH (Froh), and the heterosis coefficient based on HER (Frohet) is 0.0019. Top ROH and HER regions contain important genes related to dairy (EHHADH, CACNA1C, MICALL1, EIF3L, GTPBP1, SYNGR1, ATF4, GRAP2, FAM83F, ACO2), immunity (LIPH, TMEM41A, PEX26, CDC42EPI, CXXC5, PSD2, PURA, CYSTM1, RNF14), growth and carcass (MAGEF1, TGS1, LYN, CHCHD7, FAM110B, SDCBP, SH3BP1, GGA1, TRIOBP, PICK1, MAFF, TOMM22, MGAT3, TNRC6B, ADSL, EP300, SMDT1, MATR3) traits. These findings may provide valuable insights into the understanding of genome-wide homozygosity and heterozygosity patterns and genetic architecture of the Pakistani crossbred cattle. - Source: PubMed
Publication date: 2025/09/26
Nisa Fakhar UnUsman MuhammadAli AsadAli Muhammad BasilKaul HaibaAsif MuhammadMrode RaphaelMukhtar Zahid