Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes

Article Abstract:

The fusion of the endoplasmic reticulum (ER) membrane in yeast is controlled by the protein Cdc48, formed by the CDC48 gene. The amino acid sequence of Cdc48 is similar to that of the yeast NSF which controls docking and fusion in the secretory system. Temperature sensitive mutants in which Cdc48 is absent remain as large budded cells with the undivided nuclei in the neck between the mother and the daughter cells. This phenotype is typically of a defect in homotypic fusion where complete fusion does not take place. Cdc48 is polar and is associated with nuclear envelop and the peripheral ER.

Observations, Proteins

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Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP

Article Abstract:

A complex with subunits that aid in the specific targeting of the translocation apparatus in the membrane, a process occurring in the initial step in the translocation of a protein across the endoplasmic reticulum membrane, is examined. The translocon subcomplex comprises the Sec62p, Sec71p and Sec72p membrane proteins. The binding of a precursor to the subcomplex depends on the existence of a signal sequence and happens only when adenosine triphosphate is absent.

Polypeptides

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Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion

Article Abstract:

Research was conducted to test whether the endoplasmic reticulum (ER)-localized t-SNARE Ufe1p engages in the homotypic fusion of ER membranes. Strains were established using standard yeast genetics while the purifications of ER membranes were determined from strain MLY1600 stored at -80 degrees C. Results indicated that organelle fusion in yeast and in mammals needed the function of organelle-specific t-SNARE in a novel homomeric t-SNARE interaction.

Genetic aspects

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