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Published on: September 3, 2011
Inp1p is a peroxisomal membrane protein required for peroxisome inheritance in Saccharomyces cerevisiae
Monica Fagarasanu1, Andrei Fagarasanu, Yuen Yi C Tam
1Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Insights
Inp1p is crucial for peroxisome inheritance in yeast cells. This protein retains peroxisomes within the mother cell and influences their division, representing the first such factor identified for peroxisomes.
Area of Science:
- Cell Biology
- Organelle Inheritance
- Yeast Genetics
Background:
- Cells possess mechanisms for organelle transmission during division.
- Peroxisome inheritance mechanisms remain poorly understood.
- Inp1p, a peripheral membrane protein, influences peroxisome morphology and partitioning.
Purpose of the Study:
- To investigate the role of Inp1p in peroxisome inheritance and cell division.
- To elucidate the molecular mechanisms underlying peroxisome partitioning.
Main Methods:
- In vivo 4-dimensional video microscopy.
- Analysis of yeast cells lacking or overexpressing the INP1 gene.
- Protein localization studies.
- Co-immunoprecipitation assays.
Main Results:
- Cells lacking INP1 showed impaired peroxisome retention in the mother cell.
- Overexpression of INP1 led to immobilized peroxisomes, preventing bud partitioning.
- Inp1p localizes to peroxisomes and the cell cortex, suggesting interactions with cellular structures.
- Inp1p interacts with Pex25p, Pex30p, and Vps1p, proteins involved in peroxisome division.
Conclusions:
- Inp1p functions as a retention factor for peroxisomes within the mother cell.
- Inp1p plays a role in regulating peroxisome division.
- Inp1p is the first identified peroxisomal protein directly involved in peroxisome inheritance.
Abstract:
Cells have evolved molecular mechanisms for the efficient transmission of organelles during cell division. Little is known about how peroxisomes are inherited. Inp1p is a peripheral membrane protein of peroxisomes of Saccharomyces cerevisiae that affects both the morphology of peroxisomes and their partitioning during cell division. In vivo 4-dimensional video microscopy showed an inability of mother cells to retain a subset of peroxisomes in dividing cells lacking the INP1 gene, whereas cells overexpressing INP1 exhibited immobilized peroxisomes that failed to be partitioned to the bud. Overproduced Inp1p localized to both peroxisomes and the cell cortex, supporting an interaction of Inp1p with specific structures lining the cell periphery. The levels of Inp1p vary with the cell cycle. Inp1p binds Pex25p, Pex30p, and Vps1p, which have been implicated in controlling peroxisome division. Our findings are consistent with Inp1p acting as a factor that retains peroxisomes in cells and controls peroxisome division. Inp1p is the first peroxisomal protein directly implicated in peroxisome inheritance.
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