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Gene Review

TRAPPC3  -  trafficking protein particle complex 3

Homo sapiens

Synonyms: BET3, BET3 homolog, CDABP0066, Trafficking protein particle complex subunit 3
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Disease relevance of TRAPPC3

  • To investigate the possible involvement of Bet3 in transport events in mammalian cells, we utilized a semi-intact cell system that reconstitutes the transport of the envelope glycoprotein of vesicular stomatitis virus (VSV-G) from the ER to the Golgi apparatus [1].

High impact information on TRAPPC3

  • In a deletion strain, both Bet3p and Bet3p C80S rescue cell viability [2].
  • BET3 is a component of TRAPP, a complex involved in the tethering of transport vesicles to the cis-Golgi membrane [2].
  • A conformational change may facilitate palmitoyl extrusion from BET3 and allow the fatty acid chain to engage in intermolecular hydrophobic interactions [2].
  • A hydrophobic pocket within BET3 buries a palmitate bound through a thioester linkage to cysteine 68 [2].
  • Binding is restored by the addition of cytosol containing Bet3p [3].

Anatomical context of TRAPPC3

  • In this system, antibodies against Bet3 inhibit transport in a dose-dependent manner, and cytosol that is immunodepleted of Bet3 is also defective in this transport [1].
  • Unlike the SNAREs, which reside on multiple compartments, Bet3p is localized exclusively to Golgi membranes [3].
  • Bet3p, a component of a large novel complex called TRAPP, acts upstream of endoplasmic reticulum (ER)-Golgi SNAREs [3].
  • Bet3 is a component of the transport protein particle complex involved in vesicular trafficking to and through the Golgi complex [4].

Analytical, diagnostic and therapeutic context of TRAPPC3

  • Gel filtration analysis demonstrates that Bet3 exists in two distinct pools in the cytosol, the high-molecular-weight pool may represent the TRAPP complex, whereas the other probably represents the monomeric Bet3 [1].


  1. Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus. Loh, E., Peter, F., Subramaniam, V.N., Hong, W. J. Cell. Sci. (2005) [Pubmed]
  2. Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization. Turnbull, A.P., Kümmel, D., Prinz, B., Holz, C., Schultchen, J., Lang, C., Niesen, F.H., Hofmann, K.P., Delbrück, H., Behlke, J., Müller, E.C., Jarosch, E., Sommer, T., Heinemann, U. EMBO J. (2005) [Pubmed]
  3. TRAPP stably associates with the Golgi and is required for vesicle docking. Barrowman, J., Sacher, M., Ferro-Novick, S. EMBO J. (2000) [Pubmed]
  4. Unique self-palmitoylation activity of the transport protein particle component Bet3: a mechanism required for protein stability. Kümmel, D., Heinemann, U., Veit, M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
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