Biology subjects

Kirichenko, E.

Publications and source records attributed to Kirichenko, E..

3 recordsLinked to original sources

bioRxiv2025

FMAGJ: Fluorescence Microscopic Astrocyte Gap Junction Images Dataset

This work introduces a novel and specialized dataset of high-resolution fluorescence microscopic images focused on astrocytic gap junctions, aiming to get insights into intercellular communication in both healthy and pathological brain conditions. The dataset includes 20 z-stack image series--10 from human glioblastoma tissue and 10 from healthy rat brain tissue--each containing between 22 and 104 optical slices. These images were acquired using standardized protocols following immunofluorescence labeling with antibodies against connexin 43 (Cx43), enabling visualization of gap junction localization at the subcellular level. The dataset is tailored to support detailed morphological and quantitative analyses of gap junction networks, featuring metadata including species and localization of possible gap junctions in images provided by bounding boxes and image masks. Its structure facilitates comparative studies across physiological states and species, enhancing translational and evolutionary perspectives on astrocytic connectivity. Given the labor-intensive nature of manual gap junction quantification, this dataset serves as a resource for the development of machine learning tools capable of automating the detection and analysis of Cx43-positive signals. CCS CONCEPTSComputing methologies[~]Computer vision problems[~]Object detection * Applied computing[~]Life and medical sciences[~]Computational biology/Molecular structural biology * Software and its engineering[~]Software notations and tools[~]Software libraries and repositories

cancer biology↗

bioRxiv2022

Analysis of the Drosophila Ajuba LIM protein defines functions for distinct LIM domains

The Ajuba LIM protein Jub mediates regulation of Hippo signaling by cytoskeletal tension through interaction with the kinase Warts, and also participates in feedback regulation of junctional tension through regulation of the cytohesin Steppke. To investigate how Jub interacts with and regulates its distinct partners, we investigated the ability of Jub proteins missing different combinations of its three LIM domains to rescue jub phenotypes and to interact with -catenin, Warts and Steppke. Multiple regions of Jub contribute to its ability to bind -catenin and to localize to adherens junctions in Drosophila wing imaginal discs. Co-immunoprecipitation experiments in cultured cells identified a specific requirement for LIM2 for binding to Warts. However, in vivo, both LIM1 and LIM2, but not LIM3, were required for regulation of wing growth, Yorkie activity, and Warts localization. Conversely, LIM2 and LIM3, but not LIM1, were required for regulation of cell shape and Steppke localization in vivo, and for maximal Steppke binding in co-immunoprecipitation experiments. These observations identify distinct functions for the different LIM domains of Jub.

cell biology↗

bioRxiv2017

Tension-dependent regulation of mammalian Hippo signaling through LIMD1

Hippo signaling is regulated by biochemical and biomechanical cues that influence the cytoskeleton, but the mechanisms that mediate this have remained unclear. We show that all three mammalian Ajuba family proteins - AJUBA, LIMD1, and WTIP - exhibit tension-dependent localization to adherens junctions, and that both Lats family proteins, LATS1 and LATS2, exhibit an overlapping tension-dependent junctional localization. This localization of Ajuba and Lats family proteins is also influenced by cell density, and by Rho activation. We establish that junctional localization of Lats kinases requires LIMD1, and that LIMD1 is also specifically required for the regulation of Lats kinases and YAP by Rho. Our results identify a biomechanical pathway that contributes to regulation of mammalian Hippo signaling, establish that this occurs through tension-dependent LIMD1-mediated recruitment and inhibition of Lats kinases in junctional complexes, and identify roles for this pathway in both Rho-mediated and density-dependent regulation of Hippo signaling.

cell biology↗