Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9971044 | PMC |
| http://dx.doi.org/10.1007/s00415-022-11417-z | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The mutation in domestic cats causes variegated patches of reddish/yellow hair and is a defining signature of random X-inactivation in female tortoiseshell and calico cats. Unlike the situation for most coat color genes, there is no apparent homolog for in other mammals. We show that the is caused by a 5 kb deletion that leads to ectopic and melanocyte-specific expression of the ( ) gene.
View Article and Find Full Text PDFGRAF1 deficiency leads to defective brown adipose tissue differentiation and thermogenic response.
Sci Rep
November 2024
Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill, NC, 27599, USA.
Adipose tissue, which is crucial for the regulation of energy within the body, contains both white and brown adipocytes. White adipose tissue (WAT) primarily stores energy, while brown adipose tissue (BAT) plays a critical role in energy dissipation as heat, offering potential for therapies aimed at enhancing metabolic health. Regulation of the RhoA/ROCK pathway is crucial for appropriate specification, differentiation and maturation of both white and brown adipocytes.
View Article and Find Full Text PDFThe CYK-4 GAP domain regulates cortical targeting of centralspindlin to promote contractile ring assembly and facilitate ring dissolution.
bioRxiv
October 2024
Department of Cell & Developmental Biology, School of Biological Sciences, University of California San Diego, La Jolla, California 92093, USA.
During cytokinesis, an equatorial contractile ring partitions the cell contents. Contractile ring assembly requires an equatorial zone of active GTP-bound RhoA generated by the guanine nucleotide exchange factor ECT2. ECT2 is activated by centralspindlin, a complex composed of two molecules each of kinesin-6 and CYK4.
View Article and Find Full Text PDFAn allosteric inhibitor of RhoGAP class-IX myosins suppresses the metastatic features of cancer cells.
Nat Commun
November 2024
Institute for Biophysical Chemistry, Hannover Medical School, Hannover, Germany.
Aberrant Ras homologous (Rho) GTPase signalling is a major driver of cancer metastasis, and GTPase-activating proteins (GAPs), the negative regulators of RhoGTPases, are considered promising targets for suppressing metastasis, yet drug discovery efforts have remained elusive. Here, we report the identification and characterization of adhibin, a synthetic allosteric inhibitor of RhoGAP class-IX myosins that abrogates ATPase and motor function, suppressing RhoGTPase-mediated modes of cancer cell metastasis. In human and murine adenocarcinoma and melanoma cell models, including three-dimensional spheroid cultures, we reveal anti-migratory and anti-adhesive properties of adhibin that originate from local disturbances in RhoA/ROCK-regulated signalling, affecting actin-dynamics and actomyosin-based cell-contractility.
View Article and Find Full Text PDFRegulation and functions of the DLC family of RhoGAP proteins: Implications for development and cancer.
Cell Signal
January 2025
University of Stuttgart, Institute of Cell Biology and Immunology, Stuttgart, Germany; University of Stuttgart, Stuttgart Research Center Systems Biology, Stuttgart, Germany. Electronic address:
The DLC (Deleted in Liver Cancer) family of RhoGAP (Rho GTPase-activating) proteins has been extensively studied since the identification of the first family member nearly 30 years ago. Rho GTPase signaling is essential for various cellular processes, including cytoskeletal dynamics, cell migration, and proliferation. Members of the DLC family are key regulators of this signaling pathway, with well-established roles in development and carcinogenesis.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!