A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding.

Sohn, Kai; Orci, Lelio; Ravazzola, Mariella; Amherdt, M; Bremser, Martina; Lottspeich, Friedrich; Fiedler, K.; Helms, J. Bernd; Wieland, Felix

doi:10.1083/jcb.135.5.1239

Cited by 205 publications

(373 citation statements)

References 59 publications

Supporting

Mentioning

351

Contrasting

Unclassified

Order By: Relevance

“…The absence of Arf proteins in the purified vesicles may be surprising in light of earlier data showing suprastoichiometric levels of Arfs over COPI subunits when vesicles were produced in vitro in the presence of guanosine 5Ј-O-(3-thio)triphosphate (GTP␥S) (Serafini et al, 1991;Rothman, 1994;Sohn et al, 1996). However, it later became evident that Arf GTPase activation proteins play essential roles in vesicle biogenesis and specificity of cargo selection (Goldberg, 1998;Lee et al, 2005), making GTP hydrolysis and dissociation of Arfs from the nascent bud or vesicle likely.…”

Section: Discussionmentioning

confidence: 95%

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

Shrivastava-Ranjan

Faúndez

Fang

et al. 2008

MBoC

View full text Add to dashboard Cite

␤-Amyloid peptides (A␤) are the major component of plaques in brains of Alzheimer's patients, and are they derived from the proteolytic processing of the ␤-amyloid precursor protein (APP). The movement of APP between organelles is highly regulated, and it is tightly connected to its processing by secretases. We proposed previously that transport of APP within the cell is mediated in part through its sorting into Mint/X11-containing carriers. To test our hypothesis, we purified APP-containing vesicles from human neuroblastoma SH-SY5Y cells, and we showed that Mint2/3 are specifically enriched and that Mint3 and APP are present in the same vesicles. Increasing cellular APP levels increased the amounts of both APP and Mint3 in purified vesicles. Additional evidence supporting an obligate role for Mint3 in traffic of APP from the trans-Golgi network to the plasma membrane include the observations that depletion of Mint3 by small interference RNA (siRNA) or mutation of the Mint binding domain of APP changes the export route of APP from the basolateral to the endosomal/lysosomal sorting route. Finally, we show that increased expression of Mint3 decreased and siRNA-mediated knockdowns increased the secretion of the neurotoxic ␤-amyloid peptide, A␤ 1-40 . Together, our data implicate Mint3 activity as a critical determinant of post-Golgi APP traffic. INTRODUCTIONThe hallmark of Alzheimer's disease is the presence in brain of plaques that contain A␤ peptides, formed by the result of proteolytic processing of the ␤-amyloid precursor protein (APP). APP is a ubiquitous, single-pass transmembrane protein of unknown function that is highly expressed in brain. Processing involves the sequential actions of ␣-or ␤-plus ␥-secretases, each of which are found in multiple cellular locations (Kuentzel et al., 1993;Selkoe, 1998;Yan et al., 2001). Although processing may occur at any step, the trans-Golgi network (TGN) is the earliest site at which APP processing is thought to commence, and APP is internalized from the cell surface to endosomal compartments where ␥-secretase also acts (Selkoe et al., 1996;Greenfield et al., 1999;Lah and Levey, 2000;Bagshaw et al., 2003).The C-terminal domain of APP contains the tyrosinebased sorting motif, YENPTY, which is conserved across species and a determinant of APP traffic (Perez et al., 1999;Bonifacino and Traub, 2003;King et al., 2004). Such sorting motifs function by binding specific adaptors to facilitate their selective import into budding carriers and ensure specificity in cargo selection and coat recruitment. The highly conserved phosphotyrosine binding (PTB) domains in all three Mint proteins have been shown previously to bind directly to the YENPXY motif of APP (Borg et al., 1996(Borg et al., , 1998Zhang et al., 1997;Sastre et al., 1998;Tanahashi and Tabira, 1999;Tomita et al., 1999;Ho et al., 2002;Araki et al., 2003). Other PTB domain containing proteins have similarly been shown to bind APP, including the Fe65 (Sabo et al., 1999) family, Dab2 (Howell et al., 1999), JIP1b (King et al....

show abstract

Section: Discussionmentioning

confidence: 95%

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

Shrivastava-Ranjan

Faúndez

Fang

et al. 2008

MBoC

View full text Add to dashboard Cite

show abstract

“…To achieve their correct targeting within the early secretory pathway they are in a dynamic equilibrium to form homo-and heterodimers with each other Jenne et al, 2002). All p24 family members are type I membrane proteins and share a common structure, with a short cytoplasmic tail containing binding signals for COP I and COP II coat complexes and a luminal domain with potential secretory cargo binding capabilities Sohn et al, 1996;Dominguez et al, 1998;Muniz et al, 2000). Proteomics analysis revealed that p24 family members are major constituents of COP I-coated vesicles (Stamnes et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Mitrović

Ben-Tekaya

Koegler

et al. 2008

MBoC

119

View full text Add to dashboard Cite

Rapidly cycling proteins of the early secretory pathway can operate as cargo receptors. Known cargo receptors are abundant proteins, but it remains mysterious why their inactivation leads to rather limited secretion phenotypes. Studies of Surf4, the human orthologue of the yeast cargo receptor Erv29p, now reveal a novel function of cargo receptors. Surf4 was found to interact with endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53 and p24 proteins. Silencing Surf4 together with ERGIC-53 or silencing the p24 family member p25 induced an identical phenotype characterized by a reduced number of ERGIC clusters and fragmentation of the Golgi apparatus without effect on anterograde transport. Live imaging showed decreased stability of ERGIC clusters after knockdown of p25. Silencing of Surf4/ERGIC-53 or p25 resulted in partial redistribution of coat protein (COP) I but not Golgi matrix proteins to the cytosol and partial resistance of the cis-Golgi to brefeldin A. These findings imply that cargo receptors are essential for maintaining the architecture of ERGIC and Golgi by controlling COP I recruitment. INTRODUCTIONThe secretory pathway of higher eukaryotic cells is composed of the three membrane organelles endoplasmic reticulum (ER), ER-Golgi intermediate compartment (ERGIC), and Golgi (Bonifacino and Glick, 2004;Appenzeller-Herzog and Hauri, 2006). Maintenance of these organelles requires a balance of anterograde (secretory) and retrograde vesicular traffic. Anterograde traffic from ER to ERGIC is mediated by coat protein (COP) II vesicles that form at ER exit sites (Aridor et al., 1995;Zeuschner et al., 2006) and fuse with the ERGIC that consists of a few hundred tubulovesicular membrane clusters in vicinity of ER exit sites (AppenzellerHerzog and Hauri, 2006). Transport from ERGIC to Golgi is mediated by pleomorphic vesicles (Ben-Tekaya et al., 2005) that carry COP I (Presley et al., 1997;Scales et al., 1997), although the mechanism of their formation remains unknown. Retrograde traffic mediated by COP I vesicles can occur from ERGIC or Golgi and recycles membrane proteins that possess either dilysine signals, including ERGIC-53 and KDEL-receptor, or diphenylalanine signals, such as members of the 24 protein family. This rapid COP I-dependent recycling is distinct from the slow Golgi-to-ER recycling of Golgi resident proteins that is COP I independent and can be either constitutive or induced (Storrie, 2005).Major constituents of anterograde and retrograde transport vesicles are transmembrane cargo receptors that mediate protein sorting by linking soluble cargo on the luminal side and coat assembly on the cytoplasmic side. To date, only few cargo receptors have been studied in detail. The polytopic transmembrane protein Erv29p is known to cycle between ER and Golgi in yeast and to operate as a cargo receptor (Belden and Barlowe, 2001). Erv29p is required for efficient packaging of the glycosylated ␣-factor pheromone precursor into COP II vesicles departing from the ER. Maturation of carboxypeptidase Y...

show abstract

“…In a yeast strain defective for vesicle fusion, a p24 knockout reduced the number of COPI-coated vesicles (Stamnes et al 1995). These data suggested that type I transmembrane proteins represent membrane receptors for coatomer and are actively required for the formation of COPI vesicles (Stamnes et al 1995;Sohn et al 1996). Surprisingly, however, in yeast the deletion of all p24 proteins showed only a reduction in the rate of transport of some cargo proteins (Springer et al 2000).…”

Section: Coat Recruitmentmentioning

confidence: 68%

“…2). Binding of coatomer to these signals depends more strongly on the phenylalanine than on the dilysine residues (Fiedler et al 1996b;Sohn et al 1996). These machinery signatures are recognized exclusively by g-COP (Bethune et al 2006).…”

Section: Coat Recruitmentmentioning

confidence: 99%

See 1 more Smart Citation

COPI Budding within the Golgi Stack

Popoff

Adolf²,

Brügger³

et al. 2011

Cold Spring Harbor Perspectives in Biology

152

169

View full text Add to dashboard Cite

The Golgi serves as a hub for intracellular membrane traffic in the eukaryotic cell. Transport within the early secretory pathway, that is within the Golgi and from the Golgi to the endoplasmic reticulum, is mediated by COPI-coated vesicles. The COPI coat shares structural features with the clathrin coat, but differs in the mechanisms of cargo sorting and vesicle formation. The small GTPase Arf1 initiates coating on activation and recruits en bloc the stable heptameric protein complex coatomer that resembles the inner and the outer shells of clathrin-coated vesicles. Different binding sites exist in coatomer for membrane machinery and for the sorting of various classes of cargo proteins. During the budding of a COPI vesicle, lipids are sorted to give a liquid-disordered phase composition. For the release of a COPI-coated vesicle, coatomer and Arf cooperate to mediate membrane separation.

show abstract

A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding.

Cited by 205 publications

References 59 publications

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

Mint3/X11γ Is an ADP-Ribosylation Factor-dependent Adaptor that Regulates the Traffic of the Alzheimer's Precursor Protein from theTrans-Golgi Network

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

COPI Budding within the Golgi Stack

Contact Info

Product

Resources

About