ArticleBiochemical and biophysical research communications2015
Chlamydia trachomatis inclusion membrane protein CT850 interacts with the dynein light chain DYNLT1 (Tctex1).
Article in Biochemical and biophysical research communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 59 citations in OpenAlex.
- Inclusion Membrane Proteins ofMicroorganisms · 2026Review
- Review
- Pathogenicity and virulence ofVirulence · 2025Review
- Direct targeting of host microtubule and actin cytoskeletons by a chlamydial pathogenic effector protein.Journal of cell science · 2024Article
- Microtubules provide force to promote membrane uncoating in vacuolar escape for a cyto-invasive bacterial pathogen.Nature communications · 2024Article
- ThemBio · 2023Article
- The emerging complexity of Chlamydia trachomatis interactions with host cells as revealed by molecular genetic approaches.Current opinion in microbiology · 2023Review
- A Functional Yeast-Based Screen Identifies the Host Microtubule Cytoskeleton as a Target of NumerousInternational journal of molecular sciences · 2023Article
- The Chlamydia trachomatis IncM Protein Interferes with Host Cell Cytokinesis, Centrosome Positioning, and Golgi Distribution and Contributes to the Stability of the Pathogen-Containing Vacuole.Infection and immunity · 2023Article
- In Search of a Mechanistic Link between Chlamydia trachomatis-Induced Cellular Pathophysiology and Oncogenesis.Infection and immunity · 2023Review
- Establishing the intracellular niche of obligate intracellular vacuolar pathogens.Frontiers in cellular and infection microbiology · 2023Review
- Molecular pathogenesis ofFrontiers in cellular and infection microbiology · 2023Review
- Article
- Chlamydia repurposes the actin-binding protein EPS8 to disassemble epithelial tight junctions and promote infection.Cell host & microbe · 2022Article
- Chlamydia trachomatis suppresses host cell store-operated CaScientific reports · 2022Article
- Inclusion Membrane Growth and Composition Are Altered by Overexpression of Specific Inclusion Membrane Proteins in Chlamydia trachomatis L2.Infection and immunity · 2021Article
- An endometrial organoid model of interactions betweenJournal of cell science · 2021Article
- Got mutants? How advances in chlamydial genetics have furthered the study of effector proteins.Pathogens and disease · 2021Review
- Eukaryotic SNARE VAMP3 Dynamically Interacts with Multiple Chlamydial Inclusion Membrane Proteins.Infection and immunity · 2021Article
- Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Chlamydia trachomatis actively subverts the minus-end directed microtubule motor, dynein, to traffic along microtubule tracks to the Microtubule Organizing Center (MTOC) where it remains within a membrane bound replicative vacuole for the duration of its intracellular development. Unlike most substrates of the dynein motor, disruption of the dynactin cargo-linking complex by over-expression of the p50 dynamitin subunit does not inhibit C. trachomatis transport. A requirement for chlamydial protein synthesis to initiate this process suggests that a chlamydial product supersedes a requirement for p50 dynamitin. A yeast 2-hybrid system was used to screen the chlamydia inclusion membrane protein CT850 against a HeLa cell cDNA library and identified an interaction with the dynein light chain DYNLT1 (Tctex1). This interaction was at least partially dependent upon an (R/K-R/K-X-X-R/K) motif that is characteristic of DYNLT1 binding domains. CT850 expressed ectopically in HeLa cells localized at the MTOC and this localization is similarly dependent upon the predicted DYNLT1 binding domain. Furthermore, DYNLT1 is enriched at focal concentrations of CT850 on the chlamydial inclusion membrane that are known to interact with dynein and microtubules. Depletion of DYNLT1 disrupts the characteristic association of the inclusion membrane with centrosomes. Collectively, the results suggest that CT850 interacts with DYNLT1 to promote appropriate positioning of the inclusion at the MTOC.
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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.