Research Topics
Genomes and Genes | M P RoutSummaryAffiliation: The Rockefeller University Country: USA Publications
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Publications
Pore relations: nuclear pore complexes and nucleocytoplasmic exchangeM P Rout
Laboratory of Cellular and Structural Biology, Rockefeller University, 1230 York Ave, New York, NY 10021, USA
Essays Biochem 36:75-88. 2000..Very little is known about how the NPC mediates transport, NPC assembly and the NPC's role in regulating transport, but these areas of research are beginning to emerge...
The yeast nuclear pore complex: composition, architecture, and transport mechanismM P Rout
The Rockefeller University, New York, NY 10021, USA
J Cell Biol 148:635-51. 2000..Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport...- Isolation and characterization of subnuclear compartments from Trypanosoma brucei. Identification of a major repetitive nuclear lamina componentM P Rout
Laboratory of Cellular and Structural Biology, Rockefeller University, New York, New York 10021, USA
J Biol Chem 276:38261-71. 2001..Immunoelectron microscopy localized NUP-1 to the inner face of the nuclear envelope, suggesting that it is a major filamentous component of the trypanosome nuclear lamina... - Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteinsJ D Aitchison
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
Science 274:624-7. 1996..This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export... - The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complexU Nehrbass
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021, USA
J Cell Biol 133:1153-62. 1996..We suggest that Nup188p is one of a group of proteins that form the octagonal core structure of the NPC and thus functions in the structural organization of the NPC and nuclear envelope... - Proteins connecting the nuclear pore complex with the nuclear interiorC Strambio-de-Castillia
Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10021, USA
J Cell Biol 144:839-55. 1999..In addition, we suggest that the Tpr filaments could provide chromatin-free conduits or tracks to guide the efficient translocation of macromolecules between the nucleoplasm and the NPC... - Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transportJ D Aitchison
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021 6399, USA
J Cell Biol 131:1659-75. 1995..Transfer of nup120 delta cells to 37 degrees C resulted in the nuclear accumulation of poly(A)+ mRNA, extensive fragmentation of the nucleolus, spindle defects, and cell death... - POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelopeR W Wozniak
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021
J Cell Biol 125:31-42. 1994..However, overproduction of POM152 inhibited cell growth. When expressed in mouse 3T3 cells, POM152 was found to be localized to the pore membrane, suggesting a conserved sorting pathway between yeast and mammals... - Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152pJ D Aitchison
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021, USA
J Cell Biol 131:1133-48. 1995.... - Isolation of the yeast nuclear pore complexM P Rout
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021
J Cell Biol 123:771-83. 1993..It retains all but one of the eight known NPC proteins. In addition it contains as many as 80 uncharacterized proteins that are candidate NPC proteins... - Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexesL F Pemberton
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021
Proc Natl Acad Sci U S A 92:1187-91. 1995..We speculate that the gene product of NUP133, Nup133p, may functionally overlap with the NUP145 gene product, Nup145p, and that these proteins may be involved in maintaining the position of the NPC within the nuclear envelope... - A distinct nuclear import pathway used by ribosomal proteinsM P Rout
Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA
Cell 89:715-25. 1997..We show that the related protein Pse1p is also a karyopherin and can functionally substitute for Kap123p; both are capable of specifically directing a ribosomal nuclear localization signal reporter to the nucleus in vivo... - The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrateD M Kraemer
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021, USA
J Biol Chem 270:19017-21. 1995..Its cytoplasmic aspect implies a role for NUP159 in nuclear import... - A new family of yeast nuclear pore complex proteinsS R Wente
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021
J Cell Biol 119:705-23. 1992..We propose that subfamilies of pore complex proteins can be defined by their characteristic combinations of different modular domains... - Isolation and characterization of nuclear envelopes from the yeast SaccharomycesC Strambio-de-Castillia
Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York 10021, USA
J Cell Biol 131:19-31. 1995..Both the NEs and H-NEs were found to be competent for the in vitro posttranslational translocation of prepro-alpha-factor. They may also be suitable to investigate other ER- and NE-associated functions in cell-free systems... 
The mechanism of nucleocytoplasmic transport through the nuclear pore complexJ Tetenbaum-Novatt
Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065, USA
Cold Spring Harb Symp Quant Biol 75:567-84. 2010..Future studies of FG nups will therefore also examine their interactions between FG nups and other proteins in their surroundings...- Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodiesH J Chial
Department of Molecular, Cellular, and Developmental Biology, University of Colorado Boulder, Boulder, Colorado 80309 0347, USA
J Cell Biol 143:1789-800. 1998..We show that Ndc1p is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE... - Nup2p dynamically associates with the distal regions of the yeast nuclear pore complexD J Dilworth
Institute for Systems Biology, Seattle, Washington, 98105, USA
J Cell Biol 153:1465-78. 2001..Together, our data support a model in which Nup2p movement facilitates the transition between the import and export phases of nucleocytoplasmic transport...