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Email address      Password

Dataset Identifier
Metadata
datasetIdentifierPASS00341
datasetTypeMSMS
submitterJoern Dengjel <joern.dengjel@frias.uni-freiburg.de>
submitter_organization
lab_head_full_name
lab_head_email
lab_head_organization
lab_head_country
datasetTagYeast_Mitophagy
datasetTitleKinetic protein abundance measurements of yeast strains undergoing stationary phase mitophagy
publicReleaseDate2011-12-01 00:00:00
finalizedDate2013-10-11 07:17:39
summaryMitophagy, the autophagic degradation of mitochondria, is an important housekeeping function in eukaryotic cells and defects in mitophagy correlate with ageing phenomena and with several neurodegenerative disorders. A central mechanistic question regarding mitophagy is whether mitochondria are consumed en masse, or whether an active process segregates defective molecules from functional ones within the mitochondrial network, thus allowing a more efficient culling mechanism. Here, we combine a proteomic study with a molecular genetic and cell biology approach to determine whether such a segregation process occurs in yeast mitochondria. We find that different mitochondrial matrix proteins undergo mitophagic degradation at distinctly different rates, supporting the active segregation hypothesis. These differential degradation rates depend on mitochondrial dynamics, suggesting a mechanism coupling weak physical segregation with mitochondrial dynamics to achieve a distillation-like effect. In agreement, the rates of mitophagic degradation strongly correlate with the degree of physical segregation of specific matrix proteins.
contributorsHagai Abeliovich, Mostafa Zarei, Kristoffer T.G. Rigbolt, Richard J. Youle, and Joern Dengjel
publicationAbeliovich H, Zarei M, Rigbolt KTG, Youl RJ and Dengjel J. Involvement of mitochondrial dynamics in the segregation of mitochondrial matrix proteins during stationary phase mitophagy, Nat Commun, submitted
growthYeast cells (WT, PEP4-/-, ATG32-/-, AUP1-/-) were harvested after 1,2,3,4,and 5 days.
treatment
extractionacid extraction generated whole yeast lysate; light, medium, heavy SILAC label proteins were mixed 1:1:1
separationproteins were separated by SDS-PAGE; gel lanes were cut into 10 slices
digestionLysC digestion
acquisition
informaticsMaxQuant/Andromeda were used for protein indetification and quantification
instrumentsThermo Scientific LTQ Orbitrap XL
speciesSaccharomyces cerevisiae
massModificationsstatic: C+57.021464, variable:K+4.025107, K+8.014199
Official URL for this dataset: http://www.peptideatlas.org/PASS/PASS00341
To access files via FTP, use credentials:
Servername: ftp.peptideatlas.org
Username: PASS00341
Password: FV8467pe

Or use your browser's FTP mode: ftp://PASS00341:FV8467pe@ftp.peptideatlas.org/

Listing of files:

 290M Oct  9  2013 20101219_MZ_Hagai_pep4_Exp1_1.RAW
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 286M Oct  9  2013 20110610_JD_Strain1100_EXP_1(day123)_1.RAW
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 278M Oct  9  2013 20110610_JD_Strain1100_EXP_2(day145)_1.RAW
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 265M Oct  9  2013 20110625_MZ_Hagai_1125_Exp1(day1,2,3)_1.RAW
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 240M Oct  9  2013 20110625_MZ_Hagai_1125_Exp2(day1,4,5)_1.RAW
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 290M Oct  9  2013 20110625_MZ_Hagai_1150_Exp1(day1,2,3)_1.RAW
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 236M Oct  9  2013 20110806_MZ_Hagai_1150_EXP1(day1,2,3)_1.RAW
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 2.2K Oct  9  2013 PASS00341_DESCRIPTION-2013-09-09_064422.txt
 2.2K Oct 11  2013 PASS00341_DESCRIPTION-2013-09-11_071327.txt
 2.2K Oct 11  2013 PASS00341_DESCRIPTION-2013-09-11_071446.txt
 2.3K Oct 11  2013 PASS00341_DESCRIPTION-2013-09-11_071628.txt
 2.2K Oct 11  2013 PASS00341_DESCRIPTION.txt
  11K Oct  9  2013 read_me_experimentalDesign.txt

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