Open Daily: 10am - 10pm | Alley door pickup 10am - 7pm 3038 Hennepin Ave Minneapolis, MN
612-822-4611

  • Open Daily: 10am - 10pm
    Alley-side Pickup: 10am - 7pm

    3038 Hennepin Ave Minneapolis, MN
    612-822-4611

Open Daily: 10am - 10pm | Alley-side Pickup: 10am - 7pm
3038 Hennepin Ave Minneapolis, MN
612-822-4611
Subunit Architecture of the Yeast Dsl1p Tethering Complex and Its Interaction with Snares.

Subunit Architecture of the Yeast Dsl1p Tethering Complex and Its Interaction with Snares.

Tripathi, Arati

Paperback

Biology

Currently unavailable to order

ISBN10: 1243986565
ISBN13: 9781243986566
Publisher: Proquest Umi Dissertation Pub
Pages: 116
Weight: 0.54
Height: 0.30 Width: 7.99 Depth: 10.00
Language: English
Multiprotein tethering complexes play an important role in vesicle trafficking and have been proposed to mediate the initial contact between a vesicle and its target membrane. The Dsl1p tethering complex is a conserved heterotrimeric protein complex essential for vesicle trafficking from the Golgi to the ER. Consistent with a role in tethering, the Dsl1p complex interacts both with COPI vesicle coat proteins and with ER-localized SNAREs. However, very little is known about its structure, assembly or how it participates in vesicle targeting and membrane fusion. My thesis addresses some of these fundamental questions. Here, I report the structure of a full-length subunit of the Dsl1p complex, Tip20p. Structural comparison shows that Tip20p shares significant similarity with subunits of the exocyst complex, which functions in vesicle tethering at the plasma membrane. This finding implies a previously unanticipated structural unity, and perhaps a deeper mechanistic unity, among several of the known multisubunit tethering complexes. I have also mapped the connectivity between the subunits of the Dsl1p complex and find that an anti-parallel association between the N-terminal helices of two subunits, Tip20p and Dsl1p, is crucial for the structural integrity of the complex. Finally, I demonstrate that the Dsl1p complex has two independent binding sites for two different ER SNARE proteins, Sec20p and Use1p. My results delineate a series of protein-protein interactions capable of tethering COPI vesicles to the ER via the t-SNAREs Sec20p and Use1p.

Also in

Biology

View All