Evidence that a glycolipid tail anchors antigen 117 to the plasma membrane of Dictyostelium discoideum cells.

Sadeghi, Homayoun; Silva, A M da; Klein, Claudette

doi:10.1073/pnas.85.15.5512

Cited by 31 publications

(14 citation statements)

References 31 publications

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“…Axonin-1 mediates neuronal cell-cell adhesion through multiple homophilic interactions and is important for neurite outgrowth, axon guidance, and neurite fasciculation. The crystal structure of axonin-1 (64,65) yes (23,33) Trans-dimer (34) Adhesion (23) Cis-oligomers (33) Insects Fasciclin 1 yes (66) yes (24) Trans-dimer (67) Vertebrates T-Cadherin yes (68) yes (69) Trans-dimer (70) Axonin-1 yes (71) yes (72) Zipper (5) Signaling (50) Lattice (37) NCAM-120 yes (73) yes (74) Trans-dimer (75) IgLON family yes (76)(77)(78) yes (78) Dimers (79,80) Contactin yes (81) yes (74) no 1 Signaling (51) LFA-3 yes (82) yes (83) no 1 Signaling (44,84) CEA family yes (85) yes (86) Trans-dimer (87) Oligomers (88) has revealed a zipper-like oligomer. (5) The teeth of the zipper are divalent monomers that arise through intramolecular interactions among the four N-terminal immunoglobulin domains of the molecule (see Fig.…”

Section: Axonin-1mentioning

confidence: 99%

Reciprocal raft–receptor interactions and the assembly of adhesion complexes

Harris

Siu

2002

BioEssays

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Cell adhesion complexes are critical for the physical coordination of cell-cell interactions and the morphogenesis of tissues and organs. Many adhesion receptors are anchored to the plasma membrane by a glycosylphosphatidylinositol (GPI) moiety and are thereby partitioned into membrane rafts. In this review, we focus on reciprocal interactions between rafts and adhesion molecules, leading to receptor clustering and raft expansion and stability. A model for a three-stage adhesion complex assembly process is also proposed. First, GPI-anchored adhesion molecules are recruited into rafts, which in turn promote receptor cis-oligomerization and thereby produce precursory complexes primed for avid trans-interactions. Second, trans-interactions of the receptors cross-link and stabilize large amalgams of rafts at sites of adhesion complex assembly. Finally, the enlarged and stabilized rafts acquire enhanced abilities to recruit the cytoskeleton and induce signaling. This process exemplifies how the domain structure of the plasma membrane can impact the function of its receptors.

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Section: Axonin-1mentioning

confidence: 99%

Reciprocal raft–receptor interactions and the assembly of adhesion complexes

Harris

Siu

2002

BioEssays

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“…Expression of the chimeric protein was driven by the constitutively active actin 15 promoter. CsClpurified DNA was then transformed into D. discoideum by using the calcium phosphate method (Sadeghi et al, 1988), and G418-resistant colonies were screened for overexpression by Western blot analysis.…”

Section: Construction Of Rab7 Overexpressing Cell Linesmentioning

confidence: 99%

Evidence for a recycling role for Rab7 in regulating a late step in endocytosis and in retention of lysosomal enzymes in Dictyostelium discoideum.

Buczynski

Bush

Zhang

et al. 1997

MBoC

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The mammalian small molecular weight GTPase Rab7 (Ypt7 in yeast) has been implicated in regulating membrane traffic at postinternalization steps along the endosomal pathway. A cDNA encoding a protein 85% identical at the amino acid level to mammalian Rab7 has been cloned from Dictyostelium discoideum. Subcellular fractionation and immunofluorescence microscopy indicated that Rab7 was enriched in lysosomes, postlysosomes, and maturing phagosomes. Cell lines were generated that overexpressed Rab7 wild-type (WT), Rab7 Q67L (constitutively active form), and Rab7 T22N (dominant negative form) proteins. The Rab7 T22N cell line internalized fluid phase markers and latex beads (phagocytosis) at one-third the rate of control cells, whereas Rab7 WT and Rab7 Q67L cell lines were normal in uptake rates but exocytosed fluid phase faster than control cells. In contrast, fluid phase markers resided in acidic compartments for longer periods of time and were more slowly exocytosed from Rab7 T22N cells as compared with control cells. Light microscopy indicated that Rab7-expressing cell lines contained morphologically altered endosomal compartments. Compared with control cells, Rab7 WT-and Rab7 Q67L-expressing cells contained a reduced number of vesicles the size of postlysosomes (>2.5 ,um) and an increased number of smaller vesicles, many of which were nonacidic; in control cells, >90% of the smaller vesicles were acidic. In contrast, Rab7 T22N cells contained an increased proportion of large acidic vesicles relative to nonacidic vesicles. Radiolabel pulse-chase experiments indicated that all of the cell lines processed and targeted lysosomal a-mannosidase normally, indicating the lack of a significant role for Rab7 in the targeting pathway; however, retention of mature lysosomal hydrolases was affected in Rab7 WT and Rab7 T22N cell lines. Contrary to the results observed for the fluid phase efflux experiments, Rab7 T22N cells oversecreted a-mannosidase, whereas Rab7 WT cells retained this hydrolase as compared with control cells. These data support a model that Rab7 may regulate retrograde transport of lysosomal enzymes and the V-type H+-ATPase from postlysosomes to lysosomes coupled with the efficient release of fluid phase from cells.

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“…Acylation of inositol confers resistance to PI-PLC, an enzyme often used to diagnose GPI anchoring (Roberts et al ., 1988) . The various GPI lipid moieties described include sn-1,2dimyristylglycerol (T. brucei VSG; Ferguson et al, 1985), 1-alkyl-2-acyl glycerol (human erythrocyte acetylcholinesterase ; Roberts et al, 1988 and Leishmania majorpromastigote surface protease; Schneider et al, 1990), monoacylglycerol (T. brucei procyclic acidic repetitive protein; Field et al, 1991), and ceramide (Dictyostelium discoideum contact site A glycoprotein ; Sadeghi et al ., 1988 ;Stadler et al, 1989) . The functional significance of these structural variations is unclear.…”

mentioning

confidence: 99%

Transfer of glycosyl-phosphatidylinositol membrane anchors to polypeptide acceptors in a cell-free system.

Mayor

Menon

Cross

1991

The Journal of Cell Biology

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Abstract. Glycosylinositol phospholipid (GPI) membrane anchors are the sole means of membrane attachment of a large number of cell surface proteins, including the variant surface glycoproteins (VSGs) of the parasitic protozoan, Trypanosoma brucei. Biosynthetic data suggest that GPI-anchored proteins are synthesized with carboxy-terminal extensions that are immediately replaced by GPI, suggesting the existence of preformed GPI species available for transfer to the na-

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Evidence that a glycolipid tail anchors antigen 117 to the plasma membrane of Dictyostelium discoideum cells.

Abstract: We describe the biochemical features of the putative cell cohesion molecule antigen 117, indicating that it is anchored to the plasma membrane by a glycolipid tail. Antigen 117 can be radiolabeled with [3H]

Cited by 31 publications

References 31 publications

Reciprocal raft–receptor interactions and the assembly of adhesion complexes

Reciprocal raft–receptor interactions and the assembly of adhesion complexes

Evidence for a recycling role for Rab7 in regulating a late step in endocytosis and in retention of lysosomal enzymes in Dictyostelium discoideum.

Transfer of glycosyl-phosphatidylinositol membrane anchors to polypeptide acceptors in a cell-free system.

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