A Family of Mammalian Proteins Homologous to Yeast Sec24p

Tang, Bor Luen; Kausalya, Jaya P.; Low, Delphine Y.H.; Lock, Mei Ling; Hong, Wanjin

doi:10.1006/bbrc.1999.0574

Cited by 69 publications

(60 citation statements)

References 26 publications

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“…We used a baculovirus expression system to produce a complex of Sec23A and Sec24C (see Fig. 8, which is published as supporting information on the PNAS web site), the two isoforms that display the broadest tissue expression (19). Purification of 6xHis-Sec24C on a nickel column resulted in recovery of stoichiometric amounts of Sec23A protein, indicating that the proteins form a 1:1 complex as shown previously (20).…”

Section: Resultsmentioning

confidence: 85%

Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER

Espenshade

Yabe

2002

Proc. Natl. Acad. Sci. U.S.A.

135

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Section: Resultsmentioning

confidence: 85%

Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER

Espenshade

Yabe

2002

Proc. Natl. Acad. Sci. U.S.A.

135

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“…2, spot 15). This protein, which lacks any obvious PDZ domain, is a member of a protein complex involved in the budding of vesicles from the endoplasmic reticulum (ER) and ER-to-Golgi transport of proteins (Tang et al, 1999).…”

Section: Resultsmentioning

confidence: 99%

New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4(a) receptor splice variant: roles in receptor targeting

Joubert

Hanson

Barthet

et al. 2004

Journal of Cell Science

Self Cite

143

140

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). Most of them are scaffolding proteins that contain several structural interaction domains such as Src homology 2 (SH2) or 3 (SH3) domains, post-synapticdensity-95/disc-large/zonula-occludens-1 (PDZ) domains and Drosophila enabled and vasodilator-stimulated phosphoprotein homologous (EVH) domains. These proteins participate in the building of large submembrane protein signaling networks. We have recently isolated a complex of at least 15 proteins interacting with the C-terminal tail of the 5-HT2C receptor, using a proteomic approach combining peptide-affinity chromatography and mass spectrometry. This further supports the interaction of the GPCR C-terminus with large protein networks. Moreover, functional studies have established that the proteins that interact with the GPCR C-terminus are implicated in various GPCR functions that do not involve Gproteins. These functions include trafficking, targeting to specific subcellular compartments, clustering with effectors, fine tuning of G-protein activation and desensitization.

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“…At the stage of ER export, mammalian homologues have been described for Sec12, Sar1, Sec23, Sec24, Sec13, and Sec31 (Kuge et al, 1994;Paccaud et al, 1996;Tang et al, 1997Tang et al, , 1999Weissman et al, 2001;Stankewich et al, 2006), and all of these proteins seem to function similarly to their yeast counterparts. However, mammalian cells often have more isoforms of a given COPII component.…”

Section: Discussionmentioning

confidence: 99%

Two Mammalian Sec16 Homologues Have Nonredundant Functions in Endoplasmic Reticulum (ER) Export and Transitional ER Organization

Bhattacharyya

Glick

2007

MBoC

132

242

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Budding yeast Sec16 is a large peripheral endoplasmic reticulum (ER) membrane protein that functions in generating COPII transport vesicles and in clustering COPII components at transitional ER (tER) sites. Sec16 interacts with multiple COPII components. Although the COPII assembly pathway is evolutionarily conserved, Sec16 homologues have not been described in higher eukaryotes. Here, we show that mammalian cells contain two distinct Sec16 homologues: a large protein that we term Sec16L and a smaller protein that we term Sec16S. These proteins localize to tER sites, and an N-terminal region of each protein is necessary and sufficient for tER localization. The Sec16L and Sec16S genes are both expressed in every tissue examined, and both proteins are required in HeLa cells for ER export and for normal tER organization. Sec16L resembles yeast Sec16 in having a C-terminal conserved domain that interacts with the COPII coat protein Sec23, but Sec16S lacks such a C-terminal conserved domain. Immunoprecipitation data indicate that Sec16L and Sec16S are each present at multiple copies in a heteromeric complex. We infer that mammalian cells have preserved and extended the function of Sec16.

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A Family of Mammalian Proteins Homologous to Yeast Sec24p

Cited by 69 publications

References 26 publications

Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER

Sterols block binding of COPII proteins to SCAP, thereby controlling SCAP sorting in ER

New sorting nexin (SNX27) and NHERF specifically interact with the 5-HT4(a) receptor splice variant: roles in receptor targeting

Two Mammalian Sec16 Homologues Have Nonredundant Functions in Endoplasmic Reticulum (ER) Export and Transitional ER Organization

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