The two yeast proteins Mlp1p and Mlp2p (homologues of the vertebrate protein Tpr) are filamentous proteins attached to the nuclear face of nuclear pore complexes. Here we perform a proteomic analysis, which reveals that the two Mlps have strikingly different interacting partners, testifying to their different roles within the cell. We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope–associated yeast spindle organizer. We further show that SPB function is compromised in mlp2 mutants. Cells lacking Mlp2p form significantly smaller SPBs, accumulate aberrant SPB component-containing structures inside the nucleus, and have stochastic failures of cell division. In addition, depletion of Mlp2p is synthetically lethal with mutants impaired in SPB assembly. Based on these data, we propose that Mlp2p links the SPB to the peripheral Mlp assembly, and that this linkage is required for efficient incorporation of components into the SPB.
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18 July 2005
Article|
July 18 2005
The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
Mario Niepel,
Mario Niepel
The Rockefeller University, New York, NY 10021
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Caterina Strambio-de-Castillia,
Caterina Strambio-de-Castillia
The Rockefeller University, New York, NY 10021
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Joseph Fasolo,
Joseph Fasolo
The Rockefeller University, New York, NY 10021
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Brian T. Chait,
Brian T. Chait
The Rockefeller University, New York, NY 10021
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Michael P. Rout
Michael P. Rout
The Rockefeller University, New York, NY 10021
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Mario Niepel
The Rockefeller University, New York, NY 10021
Caterina Strambio-de-Castillia
The Rockefeller University, New York, NY 10021
Joseph Fasolo
The Rockefeller University, New York, NY 10021
Brian T. Chait
The Rockefeller University, New York, NY 10021
Michael P. Rout
The Rockefeller University, New York, NY 10021
Correspondence to M.P. Rout: [email protected] or C. Strambio-de-Castillia: [email protected]
M. Niepel and C. Strambio-de-Castillia contributed equally to this paper.
J. Fasolo's present address is Yale University, New Haven, CT 06520.
Abbreviations used: IMO, intranuclear microtubule organizer; MTOC, microtubule organizer center; NE, nuclear envelope; NPC, nuclear pore complex; PrA, protein A; SPB, spindle pole body; TEM, transmission electron microscopy.
Received:
April 26 2005
Accepted:
June 15 2005
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2005
J Cell Biol (2005) 170 (2): 225–235.
Article history
Received:
April 26 2005
Accepted:
June 15 2005
Citation
Mario Niepel, Caterina Strambio-de-Castillia, Joseph Fasolo, Brian T. Chait, Michael P. Rout; The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly . J Cell Biol 18 July 2005; 170 (2): 225–235. doi: https://doi.org/10.1083/jcb.200504140
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