Disease relevance of UFE1

• We replaced the FHV protein A mitochondrial outer membrane-targeting sequence with the N-terminal endoplasmic reticulum (ER)-targeting sequence from the yeast NADP cytochrome P450 oxidoreductase or inverted C-terminal ER-targeting sequences from the hepatitis C virus NS5B polymerase or the yeast t-SNARE Ufe1p [1].

High impact information on UFE1

• We propose that the Ufe1 protein acts in the dual capacity of an organelle membrane fusion-associated SNARE by undergoing direct t-t-SNARE and Cdc48p interactions during organelle membrane fusion as well as a t-SNARE for vesicular traffic [2].
• We present evidence that the fusion of ER membranes requires Ufe1p, a t-SNARE that localizes to the ER, but no known v-SNAREs [2].
• Organelle membrane fusion: a novel function for the syntaxin homolog Ufe1p in ER membrane fusion [2].
• Large liposomes containing bound cytoplasmic domains of the v-SNAREs, Sec22p or Bos1p, or of the ER resident proteins, Sec12p and Ufe1p, were exposed to COPII proteins and GMP-PNP. v-SNAREs but not resident proteins were concentrated in synthetic COPII vesicles generated from donor liposomes [3].
• In yeast, retrograde transport from the Golgi complex to the ER is mediated by the ER t-SNARE Ufe1p, and also requires two other ER proteins, Sec20p and Tip20p, which bind each other [4].

Biological context of UFE1

• Molecular analysis of UFE1, a Saccharomyces cerevisiae gene essential for spore formation and vegetative growth [5].
• The coding region of UFE1 is separated from the TMP1 gene on chromosome XV by 624 bp [5].
• We show that the amino acid sequence of the Ufe1p TMD is important for both function and ER targeting, and that the requirements for each are distinct [6].

Anatomical context of UFE1

• We have investigated the targeting of the yeast endoplasmic reticulum (ER) t-SNARE Ufe1p [6].
• Lengthening the Ufe1p TMD allows transport along the secretory pathway to the vacuole or plasma membrane [6].

Other interactions of UFE1

• Translation of the UFE1 coding region generates a protein with significant similarity to cytokeratin and to the coiled-coil region of SED5, USO1 and restin, suggesting that it is involved in the secretory pathway and may also be related to intermediate filament-associated proteins [5].
• Based on the previously reported association with Ufe1 and Sec22, Sec20 likely contributes the fourth SNARE to the SNAREpin [7].
• It forms a SNARE complex with Sec22 and the ER syntaxin Ufe1 [7].
• Sec20p-interacting proteins (Tip20p, Ufe1p) in the retrograde secretory pathway of the fungal pathogen Candida albicans [8].
• When the proteoliposomes were mixed with COPII proteins and GMP-PNP, Emp46/47p, but not Ufe1p, were concentrated into COPII vesicles [9].

References