Intermediate filament formation by a yeast protein essential for organelle inheritance
- PMID: 8480179
- DOI: 10.1126/science.8480179
Intermediate filament formation by a yeast protein essential for organelle inheritance
Abstract
Intermediate filaments are abundant cytoskeletal components whose specific cellular functions are poorly understood. The Saccharomyces cerevisiae protein MDM1 displays structure and solubility properties that are similar to those of intermediate filament proteins of animal cells. Yeast cells that have a mutant form of MDM1 exhibit temperature-sensitive growth and defective transfer of nuclei and mitochondria to daughter cells during incubation at the nonpermissive temperature of 37 degrees C. The purified, wild-type MDM1 protein readily forms 10-nanometer-wide filaments at either 4 degrees C or 37 degrees C. In contrast, the purified, mutant protein forms filaments at 4 degrees C but fails to form such structures at 37 degrees C. These results suggest that intermediate filament proteins are universal components of eukaryotic cells.
Similar articles
-
Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance.J Cell Biol. 1997 Aug 11;138(3):485-94. doi: 10.1083/jcb.138.3.485. J Cell Biol. 1997. PMID: 9245780 Free PMC article.
-
Nuclear and mitochondrial inheritance in yeast depends on novel cytoplasmic structures defined by the MDM1 protein.J Cell Biol. 1992 Jul;118(2):385-95. doi: 10.1083/jcb.118.2.385. J Cell Biol. 1992. PMID: 1378448 Free PMC article.
-
A role for ubiquitination in mitochondrial inheritance in Saccharomyces cerevisiae.J Cell Biol. 1999 Jun 14;145(6):1199-208. doi: 10.1083/jcb.145.6.1199. J Cell Biol. 1999. PMID: 10366593 Free PMC article.
-
Dynamic organisation of intermediate filaments and associated proteins during the cell cycle.Bioessays. 1997 Apr;19(4):297-305. doi: 10.1002/bies.950190407. Bioessays. 1997. PMID: 9136627 Review.
-
Intermediate filament assembly: fibrillogenesis is driven by decisive dimer-dimer interactions.Curr Opin Struct Biol. 1998 Apr;8(2):177-85. doi: 10.1016/s0959-440x(98)80035-3. Curr Opin Struct Biol. 1998. PMID: 9631290 Review.
Cited by
-
The Phox homology (PX) domain, a new player in phosphoinositide signalling.Biochem J. 2001 Dec 15;360(Pt 3):513-30. doi: 10.1042/0264-6021:3600513. Biochem J. 2001. PMID: 11736640 Free PMC article. Review.
-
Mutational analysis of Mdm1p function in nuclear and mitochondrial inheritance.J Cell Biol. 1997 Aug 11;138(3):485-94. doi: 10.1083/jcb.138.3.485. J Cell Biol. 1997. PMID: 9245780 Free PMC article.
-
Structural basis for different phosphoinositide specificities of the PX domains of sorting nexins regulating G-protein signaling.J Biol Chem. 2014 Oct 10;289(41):28554-68. doi: 10.1074/jbc.M114.595959. Epub 2014 Aug 22. J Biol Chem. 2014. PMID: 25148684 Free PMC article.
-
Organellar dynamics during the cell cycle of Toxoplasma gondii.J Cell Sci. 2008 May 1;121(Pt 9):1559-68. doi: 10.1242/jcs.021089. Epub 2008 Apr 14. J Cell Sci. 2008. PMID: 18411248 Free PMC article.
-
Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane.J Cell Biol. 1994 Sep;126(6):1361-73. doi: 10.1083/jcb.126.6.1361. J Cell Biol. 1994. PMID: 8089171 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases