RanGTP-Regulated Interactions of CRM1 with Nucleoporins and a Shuttling DEAD-Box Helicase
Askjaer, Peter, Bachi, Angela, Wilm, Matthias, Bischoff, F. Ralf, Weeks, Daniel L., Ogniewski, Vera, ...
CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly...
Genetic and Physical Interactions Involving the Yeast Nuclear Cap-Binding Complex
Fortes, Puri, Kufel, Joanna, Fornerod, Maarten, Polycarpou-Schwarz, Maria, Lafontaine, Denis, Tollervey, David, ...
Yeast strains lacking the yeast nuclear cap-binding complex (yCBC) are viable, although impaired in growth. We have taken advantage of this observation to carry out a genetic screen for components...
Walther, Tobias C., Fornerod, Maarten, Pickersgill, Helen, Goldberg, Martin, Allen, Terry D., Mattaj, Iain W.
The nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC...
Luc7p, a novel yeast U1 snRNP protein with a role in 5′ splice site recognition
Fortes, Puri, Bilbao-Cortés, Daniel, Fornerod, Maarten, Rigaut, Guillaume, Raymond, Wendy, Séraphin, Bertrand, ...
The characterization of a novel yeast-splicing factor, Luc7p, is presented. The LUC7 gene was identified by a mutation that causes lethality in a yeast strain lacking the nuclear cap-binding complex...
Bernad, Rafael, Van Der Velde, Hella, Fornerod, Maarten, Pickersgill, Helen
Nuclear pore complexes (NPCs) traverse the nuclear envelope (NE), providing a channel through which nucleocytoplasmic transport occurs. Nup358/RanBP2, Nup214/CAN, and Nup88 are components of the...
Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358
Engelsma, Dieuwke, Bernad, Rafael, Calafat, Jero, Fornerod, Maarten
Leucine-rich nuclear export signals (NESs) mediate rapid nuclear export of proteins via interaction with CRM1. This interaction is stimulated by RanGTP but remains of a relatively low affinity. In...
RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
Englmeier, Ludwig, Fornerod, Maarten, Bischoff, F. Ralf, Petosa, Carlo, Mattaj, Iain W., Kutay, Ulrike
We investigated the role of RanBP3, a nuclear member of the Ran-binding protein 1 family, in CRM1-mediated protein export in higher eukaryotes. RanBP3 interacts directly with CRM1 and also forms a...
RanGTP-Regulated Interactions of CRM1 with Nucleoporins and a Shuttling DEAD-Box Helicase
Askjaer, Peter, Bachi, Angela, Wilm, Matthias, Bischoff, F. Ralf, Weeks, Daniel L., Ogniewski, Vera, ...
CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly...
Genetic and Physical Interactions Involving the Yeast Nuclear Cap-Binding Complex
Fortes, Puri, Kufel, Joanna, Fornerod, Maarten, Polycarpou-Schwarz, Maria, Lafontaine, Denis, Tollervey, David, ...
Yeast strains lacking the yeast nuclear cap-binding complex (yCBC) are viable, although impaired in growth. We have taken advantage of this observation to carry out a genetic screen for components...
Walther, Tobias C., Fornerod, Maarten, Pickersgill, Helen, Goldberg, Martin, Allen, Terry D., Mattaj, Iain W.
The nuclear pore complex (NPC) is a large proteinaceous structure through which bidirectional transport of macromolecules across the nuclear envelope (NE) takes place. Nup153 is a peripheral NPC...
Luc7p, a novel yeast U1 snRNP protein with a role in 5′ splice site recognition
Fortes, Puri, Bilbao-Cortés, Daniel, Fornerod, Maarten, Rigaut, Guillaume, Raymond, Wendy, Séraphin, Bertrand, ...
The characterization of a novel yeast-splicing factor, Luc7p, is presented. The LUC7 gene was identified by a mutation that causes lethality in a yeast strain lacking the nuclear cap-binding complex...
Bernad, Rafael, Van Der Velde, Hella, Fornerod, Maarten, Pickersgill, Helen
Nuclear pore complexes (NPCs) traverse the nuclear envelope (NE), providing a channel through which nucleocytoplasmic transport occurs. Nup358/RanBP2, Nup214/CAN, and Nup88 are components of the...
Supraphysiological nuclear export signals bind CRM1 independently of RanGTP and arrest at Nup358
Engelsma, Dieuwke, Bernad, Rafael, Calafat, Jero, Fornerod, Maarten
Leucine-rich nuclear export signals (NESs) mediate rapid nuclear export of proteins via interaction with CRM1. This interaction is stimulated by RanGTP but remains of a relatively low affinity. In...
RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
Englmeier, Ludwig, Fornerod, Maarten, Bischoff, F. Ralf, Petosa, Carlo, Mattaj, Iain W., Kutay, Ulrike
We investigated the role of RanBP3, a nuclear member of the Ran-binding protein 1 family, in CRM1-mediated protein export in higher eukaryotes. RanBP3 interacts directly with CRM1 and also forms a...
RanBP3 enhances nuclear export of active β-catenin independently of CRM1
Hendriksen, Jolita, Fagotto, Francois, Van Der Velde, Hella, Van Schie, Martijn, Noordermeer, Jasprien, Fornerod, Maarten
β-Catenin is the nuclear effector of the Wnt signaling cascade. The mechanism by which nuclear activity of β-catenin is regulated is not well defined. Therefore, we used the nuclear marker RanGTP...
Pritchard, Colin E.J., Fornerod, Maarten, Kasper, Lawryn H.
Gle2p is implicated in nuclear export of poly(A)+ RNA and nuclear pore complex (NPC) structure and distribution in Saccharomyces cerevisiae. Gle2p is anchored at the nuclear envelope (NE) via a short...
Walther, Tobias C., Pickersgill, Helen S., Cordes, Volker C., Goldberg, Martin W., Allen, Terry D., Mattaj, Iain W., ...
The nuclear pore complex (NPC) mediates bidirectional macromolecular traffic between the nucleus and cytoplasm in eukaryotic cells. Eight filaments project from the NPC into the cytoplasm and are...
Roth, Peggy, Xylourgidis, Nikos, Sabri, Nafiseh, Uv, Anne, Fornerod, Maarten, Samakovlis, Christos
Many cellular responses rely on the control of nucleocytoplasmic transport of transcriptional regulators. The Drosophila nucleoporin Nup88 is selectively required for nuclear accumulation of Rel...
A Supraphysiological Nuclear Export Signal Is Required for Parvovirus Nuclear Export
Engelsma, Dieuwke, Valle, Noelia, Fish, Alexander, Salomé, Nathalie, Almendral, José M., Fornerod, Maarten
CRM1 exports proteins that carry a short leucine-rich peptide signal, the nuclear export signal (NES), from the nucleus. Regular NESs must have low affinity for CRM1 to function optimally. We...
The inner nuclear envelope as a transcription factor resting place
Heessen, Stijn, Fornerod, Maarten
Just as people head to the beaches for a well-deserved rest, accumulating evidence suggests that transcription factors take similar ‘vacations' at the nuclear envelope. Recent studies indicate that...