Distinct isocomplexes of the TRAPP trafficking factor coexist inside human cells

Kümmel, Daniel; Oeckinghaus, Andrea; Wang, Chengcheng; Krappmann, Daniel; Heinemann, Udo

doi:10.1016/j.febslet.2008.09.056

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Volume 582, Issue 27 , Pages 3729-3733, 12 November 2008

Distinct isocomplexes of the TRAPP trafficking factor coexist inside human cells

Edited by Felix Wieland

Daniel Kümmel
- Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Straβe 10, 13125 Berlin, Germany
Andrea Oeckinghaus
- Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Straβe 10, 13125 Berlin, Germany
- Helmholtz Zentrum München, German Research Center for Environmental Health, 85764 Neuherberg, Germany
Chengcheng Wang
- Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Straβe 10, 13125 Berlin, Germany
- Chemistry and Biochemistry Institute, Free University of Berlin, 14195 Berlin, Germany
Daniel Krappmann
- Helmholtz Zentrum München, German Research Center for Environmental Health, 85764 Neuherberg, Germany
Udo Heinemann
- Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Straβe 10, 13125 Berlin, Germany
- Chemistry and Biochemistry Institute, Free University of Berlin, 14195 Berlin, Germany
- Corresponding author. Address: Max-Delbrück Center for Molecular Medicine, Robert-Rössle-Straβe 10, 13125 Berlin, Germany. Fax: +49 0 30 94062548.

Received 14 August 2008; received in revised form 15 September 2008; accepted 25 September 2008. published online 17 October 2008.

Abstract

The transport protein particle (TRAPP) complex is required for proper vesicular transport from the ER to the Golgi. The composition of yeast TRAPP is well characterized, but the organization of mammalian TRAPP complex remains elusive. Using a tandem affinity purification (TAP) approach, we provide first experimental proof for the association of NIBP (NIK/IKKβ binding protein) with Bet3 and find two human paralogs of Trs33 (A and B) associated with Bet3. Interaction studies and gel filtration analysis reveal that both proteins are part of human TRAPP and might mark two distinct isocomplexes that exert different functions in the regulation of ER-to-Golgi traffic.

Structured summary

MINT-6784845:

Bet3 (uniprotkb:O43617) physically interacts (MI:0218) with Trs33B (uniprotkb:Q86SZ2) by anti bait coimmunoprecipitation (MI:0006)

MINT-6785053:

Trs33B (uniprotkb:Q86SZ2) physically interacts (MI:0218) with Bet3 (uniprotkb:O43617) and Sedl (uniprotkb:O14582) by anti bait coimmunoprecipitation (MI:0006)

MINT-6784856:

Bet3 (uniprotkb:O43617) physically interacts (MI:0218) with Trs33A2 (uniprotkb:O75865-2) by anti bait coimmunoprecipitation (MI:0006)

MINT-6785038:

Trs33A1 (uniprotkb:O75865-2) physically interacts (MI:0218) with Sedl (uniprotkb:O14582) and Bet3 (uniprotkb:O43617) by anti bait coimmunoprecipitation (MI:0006)

MINT-6784879:

Bet3 (uniprotkb:O43617) physically interacts (MI:0218) with NIBP (uniprotkb:Q96Q05) by tandem affinity purification (MI:0676)

MINT-6785068:

Trs33B (uniprotkb:Q86SZ2), Trs33A2 (uniprotkb:O75865-2) and Bet3 (uniprotkb:O43617) colocalize (MI:0403) by molecular sieving (MI:0071)

MINT-6785415:

Bet3 (uniprotkb:O43617) physically interacts (MI:0218) with Trs33A1 (uniprotkb:O75865) by anti bait coimmunoprecipitation (MI:0006)

Keywords: Vesicular transport, TRAPP, Golgi, Bet3, Trs33