Nuclear translocation and transcription regulation by the membrane-associated guanylate kinase CASK/LIN-2
Article Abstract:
It is possible that CASK/LIN-2, a membrane-associated guanylate kinase needed for EGF receptor localization and signalling in Caenorhabditis elegans, translocates from cell junction to nucleus in mature neurons. However, research in this area detected CASK only in embryonic neurons. Binding partners for the guanylate kinase domain of CASK were identified by undertaking a yeast two-hybrid screen of brain complementary DNA libraries, from which Tbr-1 was isolated. This is believed to be the first example of a membrane-associated guanylate kinase translocating into the nucleus, interacting with a defined transcription factor and controlling transcription.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2000
User Contributions:
Comment about this article or add new information about this topic:
Reduction of transcription by homologue asynapsis in Drosophila imaginal discs
Article Abstract:
Transcription studies on both alleles of the Drosophila Ultrabithorax gene reveal a complex level of trans regulation with chromosome synapsis enhancing the expression levels from both chromosomes. The results negate the predictions of simple transvection models and create a scene of gross chromosome rearrangements. These rearrangements, such as translocations, may cause global reductions in gene expression on the affected chromosome. The results may prove useful in understanding genetic disorders related to chromosome rearrangements.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
Clustering of shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases
Article Abstract:
The PSD-95 family of membrane-associated putative guanylate kinases regulates the cell-surface clustering of Shaker-type K+ channels. The regulation involves two PDZ domains of the PSD-95 protein binding to the K+ channel subunits' carboxy-terminal cytoplasmic tails. The PSD-95 proteins most likely have a larger function in the brain since they exceed the K+ channels and so may organize the surface distribution of many integral membrane proteins.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
User Contributions:
Comment about this article or add new information about this topic: