Megan C King
Affiliation: The Rockefeller University
- Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectorsStephen K Dove
School of Biosciences, University of Birmingham, Birmingham, UK
EMBO J 23:1922-33. 2004..Svp1p is not involved in the contributions of FAB1/PtdIns(3,5)P2 to MVB sorting or to vacuole acidification and so additional PtdIns(3,5)P2 effectors must exist...
- Karyopherin-mediated import of integral inner nuclear membrane proteinsMegan C King
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA
Nature 442:1003-7. 2006..We also provide evidence that specific nuclear pore complex proteins contribute to this process, suggesting a role for signal-mediated alterations in the nuclear pore complex to allow for passage of INM proteins along the pore membrane...
- A network of nuclear envelope membrane proteins linking centromeres to microtubulesMegan C King
Laboratory of Cell Biology, The Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA
Cell 134:427-38. 2008..This work highlights a framework for communication between cytoplasmic microtubules and chromatin...
- Highway to the inner nuclear membrane: rules for the roadC Patrick Lusk
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
Nat Rev Mol Cell Biol 8:414-20. 2007..Here we develop a set of rules that might govern the transport of proteins to the inner nuclear membrane...
- Inhibition of nuclear import and cell-cycle progression by mutated forms of the dynamin-like GTPase MxBMegan C King
Department of Biochemistry and Biophysics and the Graduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA
Proc Natl Acad Sci U S A 101:8957-62. 2004..These studies indicate an unexpected role for a dynamin-like protein in nucleocytoplasmic trafficking and suggest that a related function might be usurped by its antiviral relatives...
- The single transmembrane domains of ErbB receptors self-associate in cell membranesJeannine M Mendrola
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104 6059, USA
J Biol Chem 277:4704-12. 2002..Our findings suggest a role for TM domain interactions in ErbB receptor function, possibly in stabilizing inactive ligand-independent receptor dimers that have been observed by several groups...