scholarly journals Sponging of glutamate at the outer plasma membrane surface reveals roles for glutamate in development

2021 ◽  
Author(s):  
Vanessa Castro‐Rodríguez ◽  
Thomas J. Kleist ◽  
Nicoline M. Gappel ◽  
Fatiha Atanjaoui ◽  
Sakiko Okumoto ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Surface ◽  
Outer Plasma Membrane ◽  
Plasma Membrane Surface

scholarly journals Paracrystalline arrays of membrane-to-membrane cross bridges associated with the inner surface of plasma membrane

1978 ◽  
Vol 77 (2) ◽  
pp. 323-328 ◽  
Author(s):  
WW Franke ◽  
C Grund ◽  
E Schmid ◽  
E Mandelkow
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Cultured Cells ◽  
Membrane Surface ◽  
Hexagonal Lattice ◽  
Interparticle Distance ◽  
Macromolecular Complexes ◽  
Inner Surface ◽  
Cross Bridges ◽  
Plasma Membrane Surface

In cultured cells of the rat kangaroo PtK2 line, veils of the cell surface were observed which consisted of only plasma membrane and paracrystalline arrays of membrane-associated particles sandwiched in between. These membrane-to-membrane cross-bridging 9-to 11-nm wide particles were somewhat coumellar-shaped and were arranged on a hexagonal lattice with an interparticle distance of 16nm. At higher magnification, they revealed an unstained core, thus suggesting a ringlike substructure. Similar arrays of paracrystal-containing veils, which were rather variable in size and frequency, were also observed in other cultured cells. It is hypothesized that these paracrystals represent protein macromolecular complexes associated with the inner plasma membrane surface which crystallize when plasma membranes come into close intracellular contact and other components of the subsurface network are removed.

The influence of differentiation-inducing agents on plasma membrane surface characteristics of THP-1 cells

2011 ◽  
Vol 5 (2) ◽  
pp. 135-142
Author(s):  
S. V. Zubova ◽  
D. S. Kabanov ◽  
A. Yu. Ivanov ◽  
E. V. Voloshina ◽  
I. I. Proskuryakov ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Membrane Surface ◽  
Surface Characteristics ◽  
Plasma Membrane Surface

scholarly journals Agrin-Induced Phosphorylation of the Acetylcholine Receptor Regulates Cytoskeletal Anchoring and Clustering

2001 ◽  
Vol 153 (1) ◽  
pp. 1-12 ◽  
Author(s):  
Lúcia S. Borges ◽  
Michael Ferns
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Acetylcholine Receptor ◽  
Membrane Surface ◽  
Β Subunit ◽  
Wild Type ◽  
Receptor Localization ◽  
Muscle Specific Kinase ◽  
Type Receptor ◽  
Plasma Membrane Surface

At the developing neuromuscular junction, a motoneuron-derived factor called agrin signals through the muscle-specific kinase receptor to induce postsynaptic aggregation of the acetylcholine receptor (AChR). The agrin signaling pathway involves tyrosine phosphorylation of the AChR β subunit, and we have tested its role in receptor localization by expressing tagged, tyrosine-minus forms of the β subunit in mouse Sol8 myotubes. We find that agrin-induced phosphorylation of the β subunit occurs only on cell surface AChR, and that AChR-containing tyrosine-minus β subunit is targeted normally to the plasma membrane. Surface AChR that is tyrosine phosphorylated is less detergent extractable than nonphosphorylated AChR, indicating that it is preferentially linked to the cytoskeleton. Consistent with this, we find that agrin treatment reduces the detergent extractability of AChR that contains tagged wild-type β subunit but not tyrosine-minus β subunit. In addition, agrin-induced clustering of AChR containing tyrosine-minus β subunit is reduced in comparison to wild-type receptor. Thus, we find that agrin-induced phosphorylation of AChR β subunit regulates cytoskeletal anchoring and contributes to the clustering of the AChR, and this is likely to play an important role in the postsynaptic localization of the receptor at the developing synapse.

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