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The nuclear pore complex–associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly
- Source :
- The Journal of Cell Biology
- Publication Year :
- 2005
- Publisher :
- The Rockefeller University Press, 2005.
-
Abstract
- 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.
- Subjects :
- Saccharomyces cerevisiae Proteins
Cell division
Saccharomyces cerevisiae
Plasma protein binding
macromolecular substances
DNA-Directed DNA Polymerase
Spindle Apparatus
Spindle pole body
Article
Mass Spectrometry
03 medical and health sciences
0302 clinical medicine
Microscopy, Electron, Transmission
Nuclear pore
Nuclear protein
Research Articles
Metaphase
030304 developmental biology
Cytokinesis
Cell Nucleus
0303 health sciences
biology
Nuclear Proteins
Microtubule organizing center
Cell Biology
biology.organism_classification
DNA Polymerase I
Phosphoproteins
Cell biology
Nuclear Pore Complex Proteins
Cytoskeletal Proteins
Mutation
Calmodulin-Binding Proteins
030217 neurology & neurosurgery
Microtubule-Organizing Center
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 15408140 and 00219525
- Volume :
- 170
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- The Journal of Cell Biology
- Accession number :
- edsair.doi.dedup.....44b0e414f3a76fa7b1b0ac6ff708cd90