Literature DB >> 15596717

Golgi inheritance in small buds of Saccharomyces cerevisiae is linked to endoplasmic reticulum inheritance.

Catherine A Reinke1, Patrycja Kozik, Benjamin S Glick.   

Abstract

According to the cisternal maturation hypothesis, endoplasmic reticulum (ER)-derived membranes nucleate new Golgi cisternae. The yeast Saccharomyces cerevisiae offers a unique opportunity to test this idea because small buds contain both ER and Golgi structures early in the cell cycle. We previously predicted that mutants defective in ER inheritance also would show defects in Golgi inheritance. Surprisingly, studies of S. cerevisiae have not revealed the expected link between ER and Golgi inheritance. Here, we revisit this issue by generating mutant strains in which many of the small buds are devoid of detectable ER. These strains also show defects in the inheritance of both early and late Golgi cisternae. Strikingly, virtually all of the buds that lack ER also lack early Golgi cisternae. Our results fit with the idea that membranes exported from the ER coalesce with vesicles derived from existing Golgi compartments to generate new Golgi cisternae. This basic mechanism of Golgi inheritance may be conserved from yeast to vertebrate cells.

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Year:  2004        PMID: 15596717      PMCID: PMC539800          DOI: 10.1073/pnas.0408256102

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  44 in total

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Authors:  Y Du; M Pypaert; P Novick; S Ferro-Novick
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4.  Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit.

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  25 in total

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3.  Capacity of the Golgi apparatus for cargo transport prior to complete assembly.

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8.  Activation of the mitogen-activated protein kinase, Slt2p, at bud tips blocks a late stage of endoplasmic reticulum inheritance in Saccharomyces cerevisiae.

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Review 9.  Membrane traffic within the Golgi apparatus.

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10.  Noncytotoxic orange and red/green derivatives of DsRed-Express2 for whole-cell labeling.

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