Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum

Lewis, Michael; Pelham, Hugh R.B.

doi:10.1016/0092-8674(92)90476-s

Cited by 379 publications

(324 citation statements)

References 32 publications

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“…This receptor retrieves resident endoplasmic reticulum (ER) proteins from the Golgi back to the ER. The distribution of erd2 is controlled by ligand binding, suggesting that it is a signal transducing receptor (Lewis and Pelham, 1992). The erd2 protein is very similar to many G protein coupled receptors in that it spans the membrane seven times.…”

Section: Other Possible Functions For Arfmentioning

confidence: 90%

Role of heterotrimeric G proteins in membrane traffic.

Bomsel

Mostov

1992

MBoC

207

142

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Section: Other Possible Functions For Arfmentioning

confidence: 90%

Role of heterotrimeric G proteins in membrane traffic.

Bomsel

Mostov

1992

MBoC

207

142

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“…might exist also within the ER, possibly as a consequence of the differential diffusion of the molecules recyded the level of the cis-Golgi (Lippincott-Schwartz et al, 1990;Haugejorden et al, 1991;Lewis and Pelham, 1992). Data on both CSQ and calreticulin (Thomas et al, 1989;Peter et al, 1992) document the existence of additional pathways of membrane recyding, originated at various levels of the GC.…”

Section: Specializations Of the Er Luminal Contentmentioning

confidence: 99%

“…Pancreatic intracisternal granules, detected in rats after starvation or CoCl2 administration, contain disulphide-linked aggregates of zymogens and are destined to be disposed of by autophagy (Tooze et al, 1990). Analogous structures, the Russell bodies, originally described in myelomas, have been shown by transfection assays to contain mutated immunoglobulins that can neither exit from nor be degraded in the ER (Valetti et al, 1991 Lewis and Pelham, 1992). From this functional point of view, our definition of the ER (the compartment marked by BiP and PDI) is bound to include also this salvage subcompartment.…”

Section: Specializations Of the Er Luminal Contentmentioning

confidence: 99%

“…Despite the availability of a few markers, such as p53, p58, and rab2 (Schweizer et al, 1991), optimal visualization of the salvage compartment often required treatment at low temperatures or with transport perturbing drugs. Furthermore, as the localization of a transfected KDEL receptor was shown to coincide with markers of the cisGolgi (Lewis and Pelham, 1992), the salvage compartment has been envisaged as part of the latter (Mellman and Simons, 1992 (Wallace et al, 1988;Valetti et al, 1991). Similarly, the assembly of the so-called translocon (Walter, 1992) by the aggregation of membrane proteins involved in translocation of nascent polypeptides might be the essential step in the RER-SER subcompartmentalization.…”

Section: Specializations Of the Er Luminal Contentmentioning

confidence: 99%

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Endoplasmic reticulum: a dynamic patchwork of specialized subregions.

Sitia

Meldolesi

1992

MBoC

150

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“…To distinguish between these possibilities, two experiments were performed. First, we tested whether a soluble resident of the ER lumen (BiP), a protein actively retrieved from the Golgi by the KDEL receptor pathway (Bole et al, 1986;Lewis and Pelham, 1992;Orci et al, 1997), is inappropriately secreted in hSac1-depleted cell populations. This is expected if hSac1 is required for formation of COP1 vesicles that help retrieve BiP.…”

Section: Functional Distinction Between Mammalian Sac1 and Arf Depletionmentioning

confidence: 99%

The Sac1 Phosphoinositide Phosphatase Regulates Golgi Membrane Morphology and Mitotic Spindle Organization in Mammals

Liu

Boukhelifa

Tribble

et al. 2008

MBoC

130

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Phosphoinositides (PIPs) are ubiquitous regulators of signal transduction events in eukaryotic cells. PIPs are degraded by various enzymes, including PIP phosphatases. The integral membrane Sac1 phosphatases represent a major class of such enzymes. The central role of lipid phosphatases in regulating PIP homeostasis notwithstanding, the biological functions of Sac1-phosphatases remain poorly characterized. Herein, we demonstrate that functional ablation of the single murine Sac1 results in preimplantation lethality in the mouse and that Sac1 insufficiencies result in disorganization of mammalian Golgi membranes and mitotic defects characterized by multiple mechanically active spindles. Complementation experiments demonstrate mutant mammalian Sac1 proteins individually defective in either phosphoinositide phosphatase activity, or in recycling of the enzyme from the Golgi system back to the endoplasmic reticulum, are nonfunctional proteins in vivo. The data indicate Sac1 executes an essential household function in mammals that involves organization of both Golgi membranes and mitotic spindles and that both enzymatic activity and endoplasmic reticulum localization are important Sac1 functional properties. INTRODUCTIONSpatial and temporal regulation of intracellular signaling in eukaryotic cells involves the compartmentalization of membrane surfaces into discrete, albeit often transient, functional units. There are several biochemical strategies by which cells generate such units or domains. One well-established strategy uses the chemical diversity offered by phosphoinositides (PIPs), i.e., phosphorylated forms of phosphatidylinositol (PtdIns) (Majerus, 1997;Fruman et al., 1998;Strahl and Thorner, 2007). The chemical heterogeneity of individual PIP species permits the construction of chemically unique platforms on membrane surfaces that, in turn, recruit unique cohorts of proteins that drive specific biological reactions. Spatial and temporal control of such reactions requires a finely coordinated balance between the activities of the lipid kinases that produce PIPs and the activities of enzymes that degrade them. PIP turnover is catalyzed by two general classes of enzymes: phospholipases and PIP phosphatases.Although experimental scrutiny of the phospholipases has historically been more intense, recent demonstrations of the significant biological functions played by PTEN, the myotubularins, and synaptojanins highlight the general importance of PIP phosphatases (Wishart et al., 2001;Wishart and Dixon, 2002;Wenk and De Camilli, 2004).The SAC domain derives from the yeast Sac1 protein (ySac1; Cleves et al., 1989), and it represents a signature for PIP phosphatase catalytic activity . PIP phosphatases such as phosphatase and tensin homolog (mutated in multiple advanced cancers 1) (PTEN) (Maehama et al., 2001), synaptojanins (Cremona et al., 1999), and synaptojanin-like proteins (Srinivasan et al., 1997;Stolz et al., 1998) all harbor SAC domains. The prototypical member of this family, ySac1, catalyzes the dephosphoryla...

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Ligand-induced redistribution of a human KDEL receptor from the Golgi complex to the endoplasmic reticulum

Cited by 379 publications

References 32 publications

Role of heterotrimeric G proteins in membrane traffic.

Role of heterotrimeric G proteins in membrane traffic.

Endoplasmic reticulum: a dynamic patchwork of specialized subregions.

The Sac1 Phosphoinositide Phosphatase Regulates Golgi Membrane Morphology and Mitotic Spindle Organization in Mammals

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