Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway

Yamashiro, Darrell J.; Tycko, Benjamin; Fluss, S R; Maxfield, Frederick R.

doi:10.1016/0092-8674(84)90414-8

Cited by 546 publications

(501 citation statements)

References 56 publications

Supporting

Mentioning

456

Contrasting

Unclassified

Order By: Relevance

“…The simplest explanation for this difference in kinetics is that AMPA receptors that are internalized in response to insulin return more slowly to the surface. This hypothesis is consistent with our finding that AMPA receptors internalized in response to AMPA, but not in response to insulin, remain largely within a recycling endosome system, as defined by colocalization with EEA1, syntaxin 13 and TfR [32][33][34][35][36][37][38][39][40] . Unlike AMPA, insulin caused a divergence of internalized AMPA receptors out of the pathway delineated by EEA1, syntaxin 13 and TfR into a separate intracellular compartment.…”

Section: Ampa Receptor Endocytosis: Basal Regulated Recyclingsupporting

confidence: 92%

Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization

et al. 2000

View full text Add to dashboard Cite

articlesThe AMPA class of ionotropic glutamate receptors mediates most of the fast excitatory synaptic transmission in mammalian brain 1 . Changing the responsiveness of postsynaptic AMPA receptors offers a powerful way to regulate excitatory synaptic transmission. Among the mechanisms proposed for modification of AMPA receptor activity, one of the simplest is a change in the number of AMPA receptors in the postsynaptic membrane. Studies suggest that AMPA receptors can move in and out of the postsynaptic membrane on a rapid time scale (for review, see ref.2). Moreover, changes in postsynaptic membrane trafficking or in synaptic targeting of AMPA receptors have been correlated with alterations in synaptic efficacy [2][3][4][5][6][7][8][9] .In developing neurons in culture, synaptic expression of AMPA receptors is modulated over a period of days by relative levels of AMPA and NMDA receptor activity [10][11][12] . Mature neurons in culture also exhibit slow changes in synaptic AMPA receptor expression in response to chronic changes in endogenous activity 9,13,14 . On a faster time scale, induction of long-term depression (LTD) or acute application of AMPA or insulin can induce a loss of AMPA receptors from the cell surface of cultured hippocampal neurons within minutes 3,6,9,15 . Conversely, induction of long-term potentiation (LTP) and activation of CaMKII are correlated with a rapid recruitment of AMPA receptors to the postsynaptic membrane 5,8 . Thus, the synaptic content of AMPA receptors can change bidirectionally on a fast time scale and result in altered synaptic transmission.Little is known about the cell biological pathways or molecular mechanisms of postsynaptic AMPA receptor trafficking. To date, studies of AMPA receptor trafficking have focused on the presence or absence of AMPA receptors at synaptic sites, or on internal versus surface expression [3][4][5][6][7][8][9][10][15][16][17][18] . However, the multiple subunits of AMPA receptors interact differentially with diverse cytoplasmic proteins including GRIP/ABP, PICK1, NSF and SAP97, all of which have been implicated in synaptic targeting of AMPA receptors 3,5,17,[19][20][21][22][23][24][25][26][27] . The diversity of AMPA receptor protein interactions, and their regulation by phosphorylation 28 , suggest that AMPA receptor trafficking is likely to be regulated by varied mechanisms.Here we report that multiple distinct pathways exist for AMPA receptor endocytosis in cultured hippocampal neurons. We have quantified a basal rate of AMPA receptor internalization, which can be enhanced by a variety of stimuli including synaptic activity, ligand binding to AMPA receptors, insulin and calcium influx. Different internalizing stimuli use distinct intracellular signaling mechanisms, different endosomal sorting pathways and distinct sequence determinants within AMPA receptor subunits to effect AMPA receptor endocytosis. RESULTS Ligand-dependent endocytosis of AMPA receptorsTranslocation of AMPA receptors from cell surface to intracellular compartments was visu...

show abstract

Section: Ampa Receptor Endocytosis: Basal Regulated Recyclingsupporting

confidence: 92%

Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization

et al. 2000

View full text Add to dashboard Cite

show abstract

“…Equivalent GFP-fusions for these three proteins have previously been shown to be functional and traffic normally in mammalian cells and/or C. elegans. First we expressed the human transferrin receptor (hTfR-GFP), a marker for clathrin-dependent uptake and rme-1-dependent recycling in mammalian cells (Yamashiro et al, 1984;Burack et al, 2000;Lin et al, 2001). Next we expressed the ␣-chain of the human IL-2 receptor TAC (hTAC-GFP), a marker for clathrin-independent endocytosis and rme-1-dependent recycling in mammalian cells (Caplan et al, 2002;Naslavsky et al, 2004).…”

Section: Gum-1 Mutants Display Rme-1-like Endocytosis Defects In the mentioning

confidence: 99%

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

Chen

Schweinsberg

Vashist

et al. 2006

MBoC

183

374

View full text Add to dashboard Cite

The endocytic pathway of eukaryotes is essential for the internalization and trafficking of macromolecules, fluid, membranes, and membrane proteins. One of the most enigmatic aspects of this process is endocytic recycling, the return of macromolecules (often receptors) and fluid from endosomes to the plasma membrane. We have previously shown that the EH-domain protein RME-1 is a critical regulator of endocytic recycling in worms and mammals. Here we identify the RAB-10 protein as a key regulator of endocytic recycling upstream of RME-1 in polarized epithelial cells of the Caenorhabditis elegans intestine. rab-10 null mutant intestinal cells accumulate abnormally abundant RAB-5-positive early endosomes, some of which are enlarged by more than 10-fold. Conversely most RME-1-positive recycling endosomes are lost in rab-10 mutants. The abnormal early endosomes in rab-10 mutants accumulate basolaterally recycling transmembrane cargo molecules and basolaterally recycling fluid, consistent with a block in basolateral transport. These results indicate a role for RAB-10 in basolateral recycling upstream of RME-1. We found that a functional GFP-RAB-10 reporter protein is localized to endosomes and Golgi in wild-type intestinal cells consistent with a direct role for RAB-10 in this transport pathway. INTRODUCTIONEndocytosis and endocytic trafficking controls the uptake and sorting of extracellular macromolecules as well as the components of the cell membrane itself, counterbalancing secretion and allowing a complex interplay between cells and their environment that is important for a myriad of cellular activities (Brodsky et al., 2001;Maxfield and McGraw, 2004). The steps involved in the uptake and trafficking of cargo within the endosomal system have been well described, but many of the components mediating these steps at the molecular level remain to be identified (Brodsky et al., 2001;Maxfield and McGraw, 2004). Many receptors and their associated ligands cluster into clathrincoated pits, whereas other types of cargo utilize clathrinindependent uptake mechanisms (Nichols, 2003;Gesbert et al., 2004). Plasma membrane invaginations pinch off into vesicles, uncoat, and then fuse with one another and with early endosomes. In early endosomes some ligand-receptor complexes dissociate because of the reduced pH of the endosomal lumen (Mukherjee et al., 1997). Many receptors then recycle to the plasma membrane (PM) either directly or indirectly via recycling endosomes (Mukherjee et al., 1997;Maxfield and McGraw, 2004). Many ligands do not recycle but instead are transported from early to late endosomes and eventually to lysosomes for degradation (Mukherjee et al., 1997). In polarized epithelial cells such as cultured Madin-Darby canine kidney (MDCK) cells, an additional layer of complexity in the endocytic pathway contributes to formation and/or maintenance of the specialized apical and basolateral domains (Nelson and Yeaman, 2001;Mostov et al., 2003;Hoekstra et al., 2004). Both the apical and basolateral membranes deliver cargo ...

show abstract

“…For these studies, we used Chinese hamster ovary (CHO) cells, in which the recycling endosome is well characterized and shown to be highly concentrated in the pericentriolar region (Yamashiro et al, 1984;Ghosh and Maxfield, 1995;Marsh et al, 1995). FITC-labeled transferrin was internalized continuously for 30 min, conditions under which the main compartment labeled is the pericentriolar recycling endosome (Ullrich et al, 1996).…”

Section: Eea1 Does Not Associate With the Recycling Endosomementioning

confidence: 99%

“…Markers first enter the early sorting endosome, a complex organelle with tubular and multivesicular domains, where membrane proteins destined for degradation are sorted away from those proteins, such as the transferrin receptor, that are recycled back to the plasma membrane. Recycling proteins can then enter a second subcompartment, termed the recycling endosome, which has a tubular morphology and in many cell types is located in the pericentriolar area of the cell (Yamashiro et al, 1984;Dunn et al, 1989;Ghosh and Maxfield, 1995). Further complexity is added to this picture by the finding that fibroblasts, generally regarded as nonpolarized cells, may contain two sets of early endosomes analogous to those in polarized cells (Wilson and Colton, 1997).…”

Section: Introductionmentioning

confidence: 99%

EEA1, a Tethering Protein of the Early Sorting Endosome, Shows a Polarized Distribution in Hippocampal Neurons, Epithelial Cells, and Fibroblasts

Wilson

Hoop

Zorzi

et al. 2000

MBoC

179

148

View full text Add to dashboard Cite

EEA1 is an early endosomal Rab5 effector protein that has been implicated in the docking of incoming endocytic vesicles before fusion with early endosomes. Because of the presence of complex endosomal pathways in polarized and nonpolarized cells, we have examined the distribution of EEA1 in diverse cell types. Ultrastructural analysis demonstrates that EEA1 is present on a subdomain of the early sorting endosome but not on clathrin-coated vesicles, consistent with a role in providing directionality to early endosomal fusion. Furthermore, EEA1 is associated with filamentous material that extends from the cytoplasmic surface of the endosomal domain, which is also consistent with a tethering/docking role for EEA1. In polarized cells (Madin-Darby canine kidney cells and hippocampal neurons), EEA1 is present on a subset of "basolateral-type" endosomal compartments, suggesting that EEA1 regulates specific endocytic pathways. In both epithelial cells and fibroblastic cells, EEA1 and a transfected apical endosomal marker, endotubin, label distinct endosomal populations. Hence, there are at least two distinct sets of early endosomes in polarized and nonpolarized mammalian cells. EEA1 could provide specificity and directionality to fusion events occurring in a subset of these endosomes in polarized and nonpolarized cells. INTRODUCTIONAnimal cells are continuously internalizing proteins and lipids of their plasma membrane via endocytosis. The internalized surface components enter a complex and dynamic membrane system, the early endosome, which plays a vital role in sorting endocytosed proteins to different destinations in the cell (Gruenberg and Maxfield, 1995). It is now clear that the early endosome comprises at least two functionally distinct compartments or subdomains (Ghosh et al., 1994;Ghosh and Maxfield, 1995;Gruenberg and Maxfield, 1995;Ullrich et al., 1996;Zacchi et al., 1998). Markers first enter the early sorting endosome, a complex organelle with tubular and multivesicular domains, where membrane proteins destined for degradation are sorted away from those proteins, such as the transferrin receptor, that are recycled back to the plasma membrane. Recycling proteins can then enter a second subcompartment, termed the recycling endosome, which has a tubular morphology and in many cell types is located in the pericentriolar area of the cell (Yamashiro et al., 1984;Dunn et al., 1989;Ghosh and Maxfield, 1995). Further complexity is added to this picture by the finding that fibroblasts, generally regarded as nonpolarized cells, may contain two sets of early endosomes analogous to those in polarized cells (Wilson and Colton, 1997). In these studies, endotubin, a membrane protein of the apical early endosomal compartment in neonatal rat intestine (Wilson et al., 1987), was heterologously expressed in normal rat kidney (NRK) cells and shown to associate with an apparently unique early endosomal compartment. This compartment was distinct from transferrin-containing early endosomes and was relatively insensitive to brefeldi...

show abstract

Segregation of transferrin to a mildly acidic (pH 6.5) para-golgi compartment in the recycling pathway

Cited by 546 publications

References 56 publications

Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization

Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

EEA1, a Tethering Protein of the Early Sorting Endosome, Shows a Polarized Distribution in Hippocampal Neurons, Epithelial Cells, and Fibroblasts

Contact Info

Product

Resources

About