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Meiringer CT, et al.  (2011) The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J Biol Chem 286(28):25039-46

Abstract: Retrograde vesicular transport from the Golgi to the ER requires the Dsl1 tethering complex, which consists of the three subunits Dsl1, Dsl3, and Tip20. It forms a stable complex with the SNAREs Ufe1, Use1, and Sec20 to mediate fusion of COPI vesicles with the endoplasmic reticulum. Here, we analyze molecular interactions between five SNAREs of the ER (Ufe1, Use1, Sec20, Sec22, and Ykt6) and the Dsl1 complex in vitro and in vivo. Of the two R-SNAREs, Sec22 is preferred over Ykt6 in the Dsl-SNARE complex. The NSF homolog Sec18 can displace Ykt6 but not Sec22, suggesting a regulatory function for Ykt6. In addition, our data also reveal that subunits of the Dsl1 complex (Dsl1, Dsl3, and Tip20), as well as the SNAREs Ufe1 and Sec20, are ER-resident proteins that do not seem to move into COPII vesicles. Our data support a model, in which a tethering complex is stabilized at the organelle membrane by binding to SNAREs, recognizes the incoming vesicle via its coat and then promotes its SNARE-mediated fusion.

Status: Published Type: Journal Article | Research Support, Non-U.S. Gov't PubMed ID: 21550981

Topics addressed in this paper

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Topics Genes linked to topics (#1 - 10 )
BOS1 DSL1 RET2 SEC17 SEC18 SEC20 SEC22 SEC39 SED5 SLY1
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Topics Genes linked to topics (#11 - 15 )
TIP20 UFE1 USE1 YKT6 YPT1
Additional Literature blue ball
Cellular Location blue ball blue ball
Function/Process blue ball blue ball blue ball
Genetic Interactions blue ball
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Protein Physical Properties blue ball blue ball blue ball blue ball
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