Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC12 cells

Sa, Green; Kelly, RB

doi:10.1083/jcb.117.1.47

Cited by 146 publications

(52 citation statements)

References 65 publications

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“…Studies of intracellular trafficking indicate that 8 hr is sufficient for endocytosed material to reach biosynthetic pathways like SER/TGN in cultured cells (Green and Kelly, 1992). Thus, these experiments further support the view that the organelles undergoing CEDE are TGN-derived structures and part of the biosynthetic pathway.…”

Section: Calcium-evoked Dendritic Exocytosissupporting

confidence: 71%

Calcium-Evoked Dendritic Exocytosis in Cultured Hippocampal Neurons. Part I: Trans-Golgi Network-Derived Organelles Undergo Regulated Exocytosis

1998

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Exocytosis is a widely observed cellular mechanism for delivering transmembrane proteins to the cell surface and releasing signaling molecules into the extracellular space. Calciumevoked exocytosis, traditionally thought to be restricted to presynaptic specializations in neurons, has been described recently in many cells. Here, calcium-evoked dendritic exocytosis (CEDE) is visualized in living cultured hippocampal neurons. Organelles that undergo CEDE are in somata, dendrites, and perisynaptic regions, identified by using immunocytochemistry and correlative light and electron microscopy. CEDE is regulated developmentally: neurons Ͻ9 d in vitro do not show CEDE. In addition, CEDE is blocked by tetanus toxin, an inhibitor of regulated exocytosis, and nocodazole, an inhibitor of microtubule polymerization. Organelles that undergo CEDE often are found on the base of spines, putative sites of synaptic plasticity. CEDE therefore could be involved in structural and functional modification of spines and could play a role in synaptic plasticity, where it might involve changes in receptor/ channel density, release of active compounds having effect on pre-and postsynaptic function, and/or growth of synaptic structures.

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Section: Calcium-evoked Dendritic Exocytosissupporting

confidence: 71%

Calcium-Evoked Dendritic Exocytosis in Cultured Hippocampal Neurons. Part I: Trans-Golgi Network-Derived Organelles Undergo Regulated Exocytosis

1998

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“…For example, the cation-independent mannose 6-phosphate receptor and the low-density lipoprotein receptor are transported to the Golgi apparatus with t1/2 = 2-3 h. Because the half-life of the proteins is >20 h, this relatively rapid recycling indicates that the receptors can return to the Golgi several times in their life span (Green and Kelly, 1992).…”

Section: Discussionmentioning

confidence: 99%

Divergent fates of P- and E-selectins after their expression on the plasma membrane.

Subramaniam

Koedam

Wagner

1993

MBoC

173

114

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P-selectin and E-selectin are related adhesion receptors for monocytes and neutrophils that are expressed by stimulated endothelial cells. P-selectin is stored in Weibel-Palade bodies, and it reaches the plasma membrane after exocytosis of these granules. E-selectin is not stored, and its synthesis is induced by cytokines. We studied the fate of the two proteins after their surface expression by following the intracellular routing of internalized antibodies to the selectins. By immunofluorescent staining, P-selectin antibody was first seen in endosomes, then in the Golgi region, and finally in Weibel-Palade bodies. In contrast, the E-selectin antibody was detected only in endosomes and lysosomes. Subcellular fractionation of cells after 4 h chase confirmed the localization of P-selectin antibody in storage granules and of the E-selectin antibody in lysosomes. In AtT-20 cells, a mouse pituitary cell line, transfected with P- or E-selectin, only P-selectin was delivered to the endogenous adrenocorticotrophic hormone storage granules after endocytosis. Deletion of the cytoplasmic domain abolished internalization. In summary, after a brief surface exposure, internalized E-selectin is degraded in the lysosomes, whereas P-selectin returns to the storage granules from where it can be reused.

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“…After unbound HRP-conjugated secondary antibodies were washed off, the filters were washed twice with PBS, impregnated with ECL substrate (Amersham, Arlington Heights, IL), and exposed to x-ray film. Biotinylated proteins transferred to Immobilon (Millipore, Bedford, MA) were detected using 125 I-streptavidin as described (Lisanti et al, 1988;Green and Kelly, 1992), and radioactive streptavidin bound to the bands was quantitated using the PhosphorImager. …”

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confidence: 99%

An Atypical Sorting Determinant in the Cytoplasmic Domain of P-Selectin Mediates Endosomal Sorting

Straley

Daugherty

Aeder

et al. 1998

MBoC

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We previously identified the 11 amino acid C1 region of the cytoplasmic domain of P-selectin as essential for an endosomal sorting event that confers rapid turnover on P-selectin. The amino acid sequence of this region has no obvious similarity to other known sorting motifs. We have analyzed the sequence requirements for endosomal sorting by measuring the effects of site-specific mutations on the turnover of P-selectin and of the chimeric protein LLP, containing the lumenal and transmembrane domains of the low density lipoprotein receptor and the cytoplasmic domain of P-selectin. Endosomal sorting activity was remarkably tolerant of alanine substitutions within the C1 region. The activity was eliminated by alanine substitution of only one amino acid residue, leucine 768, where substitution with several other large side chains, hydrophobic and polar, maintained the sorting activity. The results indicate that the endosomal sorting determinant is not structurally related to previously reported sorting determinants. Rather, the results suggest that the structure of the sorting determinant is dependent on the tertiary structure of the cytoplasmic domain. INTRODUCTIONThe function of membrane-bounded organelles requires correct targeting of resident membrane proteins to each organelle and in many cases selective cycling of membrane proteins between organelles. Selective localization and targeting of membrane proteins to their appropriate destinations depend on structural features of these proteins, termed sorting determinants. Sorting determinants are recognized by sorting machinery that functions to concentrate proteins bearing the appropriate sorting determinants into specific transport vesicles, which can then carry their cargo vectorially to the correct destination. A number of sorting determinants have been characterized, including those that mediate localization to clathrin-coated pits in the trans-Golgi network (TGN) 11 or at the cell surface, sorting to the basolateral cell surface in polarized epithelial cells, and selective transport from endosomes to lysosomes (Sandoval and Bakke, 1994;Mellman, 1996;Kirchhausen et al., 1997;Marks et al., 1997).Many sorting determinants are contained in short segments of amino acid sequence in the cytoplasmic domains of transmembrane proteins (Sandoval and Bakke, 1994;Marks et al., 1997). These short sequences have been defined by mutagenesis experiments in which systematic substitution of amino acid residues identifies only a few mutations that disrupt sorting activity. To date, the most prevalent and most extensively studied determinants that operate in post-Golgi trafficking pathways are those that require a tyrosine residue and additional residues in specific contexts * Present address: Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, VA 22908. † Corresponding author: Department of Cell Biology, Box 439 HSC, University of Virginia, Charlottesville VA 22908. E-mail address: sag4y@virginia.edu. 1 Abbreviations used: CHO, Ch...

show abstract

Low density lipoprotein receptor and cation-independent mannose 6-phosphate receptor are transported from the cell surface to the Golgi apparatus at equal rates in PC12 cells

Cited by 146 publications

References 65 publications

Calcium-Evoked Dendritic Exocytosis in Cultured Hippocampal Neurons. Part I: Trans-Golgi Network-Derived Organelles Undergo Regulated Exocytosis

Calcium-Evoked Dendritic Exocytosis in Cultured Hippocampal Neurons. Part I: Trans-Golgi Network-Derived Organelles Undergo Regulated Exocytosis

Divergent fates of P- and E-selectins after their expression on the plasma membrane.

An Atypical Sorting Determinant in the Cytoplasmic Domain of P-Selectin Mediates Endosomal Sorting

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