Reactome | SEC16 complex binds SAR1B:GTP:SEC23:SEC24

SEC16 complex binds SAR1B:GTP:SEC23:SEC24

Stable Identifier

R-HSA-5694417

Type

Reaction [binding]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

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Metabolism of proteins (Homo sapiens)

- Post-translational protein modification (Homo sapiens)
  - Asparagine N-linked glycosylation (Homo sapiens)
    - Transport to the Golgi and subsequent modification (Homo sapiens)
      - ER to Golgi Anterograde Transport (Homo sapiens)
        
        COPII-mediated vesicle transport (Homo sapiens)
        
        SEC16 complex binds SAR1B:GTP:SEC23:SEC24 (Homo sapiens)

General

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SEC16 complex binds SAR1B:GTP:SEC23:SEC24

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The multimeric SEC16 complex marks sites of ER exit (ERES) and helps to localize nascent COPII coat complexes through interaction with SEC23 and SAR1 (Battacharyya et al, 2007; Watson et al, 2006; Hughes et al, 2009; Yorimitsu and Sato, 2012; reviewed in Sprangers and Rabouille, 2015). SEC16 may help to prevent premature dissociation of the COPII coats after activation of SEC13 GTPase (Supek et al, 2002; Kung et al, 2012). SEC16 functions with hexameric TFG1, which is recruited to the ERES through direct interaction with SEC16 and is required for cargo traffic out of the ER and for organization of the ER-to-ERGIC boundary (Witte et al, 2001; Beetz et al, 2012; Johnson et al, 2015).

Literature References

PubMed ID	Title	Journal	Year
22157747	Sec24p and Sec16p cooperate to regulate the GTP cycle of the COPII coat Pagant, S, Kung, LF, D'Arcangelo, JG, Hamamoto, S, Miller, EA, Schekman, R, Reid, RJ, Futai, E, Buchanan, R, Snapp, EL, Rothstein, R, Dittmar, JC	EMBO J.	2012
23479643	Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure Saxena, R, Schuh, AL, Altmüller, J, Beetz, C, Nürnberg, P, Audhya, A, Thiele, H, Chapman, ER, Nürnberg, G, Bomba-Warczak, E, Thakur, S, Varga, RE, Fothergill, T, Dent, EW, Johnson, A, Hertel, N	Proc. Natl. Acad. Sci. U.S.A.	2013
25619252	SEC16 in COPII coat dynamics at ER exit sites Rabouille, C, Sprangers, J	Biochem. Soc. Trans.	2015
25586378	TFG clusters COPII-coated transport carriers and promotes early secretory pathway organization Audhya, A, Otegui, MS, Bhattacharya, N, Hanna, M, Schuh, AL, Wang, L, Stagg, SM, Pennington, JG, Johnson, A	EMBO J.	2015
12235121	Sec16p potentiates the action of COPII proteins to bud transport vesicles Madden, DT, Orci, L, Hamamoto, S, Supek, F, Schekman, R	J. Cell Biol.	2002
17192411	Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization Bhattacharyya, D, Glick, BS	Mol. Biol. Cell	2007
17005010	Sec16 defines endoplasmic reticulum exit sites and is required for secretory cargo export in mammalian cells Stephens, DJ, Palmer, KJ, Townley, AK, Koka, P, Watson, P	Traffic	2006
19638414	Organisation of human ER-exit sites: requirements for the localisation of Sec16 to transitional ER Carter, DA, Verkade, P, Schmidt, K, Stephens, DJ, Mantell, J, Johnson, A, Palmer, KJ, Hughes, H, Budnik, A, Noakes, C, Watson, P	J. Cell. Sci.	2009
21478858	TFG-1 function in protein secretion and oncogenesis Eimer, S, Audhya, A, Witte, K, Sarkeshik, A, Yates, JR, Schuh, AL, Mayers, JR, Hegermann, J, Schwarze, K	Nat. Cell Biol.	2011
22675024	Insights into structural and regulatory roles of Sec16 in COPII vesicle formation at ER exit sites Sato, K, Yorimitsu, T	Mol. Biol. Cell	2012