scholarly journals Binding Site for Chitin Oligosaccharides in the Soybean Plasma Membrane

2001 ◽  
Vol 126 (3) ◽  
pp. 1162-1173 ◽  
Author(s):  
R. Bradley Day ◽  
Mitsuo Okada ◽  
Yuki Ito ◽  
Koji Tsukada ◽  
Habib Zaghouani ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Site

Inhibition of clathrin-coated pit assembly by an Eps15 mutant

1999 ◽  
Vol 112 (9) ◽  
pp. 1303-1311 ◽  
Author(s):  
A. Benmerah ◽  
M. Bayrou ◽  
N. Cerf-Bensussan ◽  
A. Dautry-Varsat
Keyword(s):  
Plasma Membrane ◽  
Fusion Protein ◽  
Binding Site ◽  
Specific Marker ◽  
Coated Pits ◽  
Receptor Mediated Endocytosis ◽  
Gfp Fusion Protein ◽  
Protein Encoding ◽  
Homology Domains

Recent data have shown that Eps15, a newly identified component of clathrin-coated pits constitutively associated with the AP-2 complex, is required for receptor-mediated endocytosis. However, its precise function remains unknown. Interestingly, Eps15 contains three EH (Eps15-Homology) domains also found in proteins required for the internalization step of endocytosis in yeast. Results presented here show that EH domains are required for correct coated pit targeting of Eps15. Furthermore, when cells expressed an Eps15 mutant lacking EH domains, the plasma membrane punctate distribution of both AP-2 and clathrin was lost, implying the absence of coated pits. This was further confirmed by the fact that dynamin, a GTPase found in coated pits, was homogeneously redistributed on the plasma membrane and that endocytosis of transferrin, a specific marker of clathrin-dependent endocytosis, was strongly inhibited. Altogether, these results strongly suggest a role for Eps15 in coated pit assembly and more precisely a role for Eps15 in the docking of AP-2 onto the plasma membrane. This hypothesis is supported by the fact that a GFP fusion protein encoding the ear domain of (alpha)-adaptin, the AP-2 binding site for Eps15, was efficiently targeted to plasma membrane coated pits.

scholarly journals The Binding Site for Regulatory 14-3-3 Protein in Plant Plasma Membrane H+-ATPase

2003 ◽  
Vol 278 (43) ◽  
pp. 42266-42272 ◽  
Author(s):  
Anja T. Fuglsang ◽  
Jonas Borch ◽  
Katrine Bych ◽  
Thomas P. Jahn ◽  
Peter Roepstorff ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Plant Plasma Membrane

The Hyaluronate-Binding Site from the Plasma Membrane is Distinct from the Binding Protein Present in Brain

1987 ◽  
Vol 16 (3) ◽  
pp. 225-235 ◽  
Author(s):  
Charles B. Underhill ◽  
Guido Tarone ◽  
Annamaria T. Kausz
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Binding Protein

scholarly journals The Calmodulin-binding Site of Sphingosine Kinase and Its Role in Agonist-dependent Translocation of Sphingosine Kinase 1 to the Plasma Membrane

2006 ◽  
Vol 281 (17) ◽  
pp. 11693-11701 ◽  
Author(s):  
Catherine M. Sutherland ◽  
Paul A. B. Moretti ◽  
Niamh M. Hewitt ◽  
Christopher J. Bagley ◽  
Mathew A. Vadas ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Sphingosine Kinase ◽  
Sphingosine Kinase 1 ◽  
Calmodulin Binding

scholarly journals Plasma membrane association of Acanthamoeba myosin I.

1989 ◽  
Vol 109 (4) ◽  
pp. 1519-1528 ◽  
Author(s):  
H Miyata ◽  
B Bowers ◽  
E D Korn
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Heavy Chain ◽  
Membrane Fraction ◽  
Plasma Membranes ◽  
Actin Binding ◽  
Plasma Membrane Fraction ◽  
Myosin I ◽  
Membrane Bound ◽  
Actin Binding Site

Myosin I accounted for approximately 2% of the protein of highly purified plasma membranes, which represents about a tenfold enrichment over its concentration in the total cell homogenate. This localization is consistent with immunofluorescence analysis of cells that shows myosin I at or near the plasma membrane as well as diffusely distributed in the cytoplasm with no apparent association with cytoplasmic organelles or vesicles identifiable at the level of light microscopy. Myosin II was not detected in the purified plasma membrane fraction. Although actin was present in about a tenfold molar excess relative to myosin I, several lines of evidence suggest that the principal linkage of myosin I with the plasma membrane is not through F-actin: (a) KI extracted much more actin than myosin I from the plasma membrane fraction; (b) higher ionic strength was required to solubilize the membrane-bound myosin I than to dissociate a complex of purified myosin I and F-actin; and (c) added purified myosin I bound to KI-extracted plasma membranes in a saturable manner with maximum binding four- to fivefold greater than the actin content and with much greater affinity than for pure F-actin (apparent KD of 30-50 nM vs. 10-40 microM in 0.1 M KCl plus 2 mM MgATP). Thus, neither the MgATP-sensitive actin-binding site in the NH2-terminal end of the myosin I heavy chain nor the MgATP-insensitive actin-binding site in the COOH-terminal end of the heavy chain appeared to be the principal mechanism of binding of myosin I to plasma membranes through F-actin. Furthermore, the MgATP-sensitive actin-binding site of membrane-bound myosin I was still available to bind added F-actin. However, the MgATP-insensitive actin-binding site appeared to be unable to bind added F-actin, suggesting that the membrane-binding site is near enough to this site to block sterically its interaction with actin.

Evidence for a binding site on the sperm plasma membrane which recognizes the murine zona pellucida: A binding site on the sperm plasma membrane

1986 ◽  
Vol 14 (3) ◽  
pp. 235-243 ◽  
Author(s):  
Gary R. Poirier ◽  
Roderick Robinson ◽  
Richard Richardson ◽  
Kathy Hinds ◽  
Deborah Clayton
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Zona Pellucida ◽  
Sperm Plasma Membrane

scholarly journals Nuclear Export and Plasma Membrane Recruitment of the Ste5 Scaffold Are Coordinated with Oligomerization and Association with Signal Transduction Components

2003 ◽  
Vol 14 (6) ◽  
pp. 2543-2558 ◽  
Author(s):  
Yunmei Wang ◽  
Elaine A. Elion
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Binding Site ◽  
Nuclear Export ◽  
Mutational Analysis ◽  
Active Form ◽  
Mitogen Activated Protein Kinase ◽  
Mitogen Activated Protein ◽  
Kinase Cascade ◽  
Protein Kinase Cascade

The Ste5 scaffold activates an associated mitogen-activated protein kinase cascade by binding through its RING-H2 domain to a Gβγ dimer (Ste4/Ste18) at the plasma membrane in a recruitment event that requires prior nuclear shuttling of Ste5. Genetic evidence suggests that Ste5 must oligomerize to function, but its impact on Ste5 function and localization is unknown. Herein, we show that oligomerization affects Ste5 activity and localization. The majority of Ste5 is monomeric, suggesting that oligomerization is tightly regulated. Increasing the pool of Ste5 oligomers increases association with Ste11. Remarkably, Ste5 oligomers are also more efficiently exported from the nucleus, retained in the cytoplasm by Ste11 and better recruited to the plasma membrane, resulting in constitutive activation of the mating mitogen-activated protein kinase cascade. Coprecipitation tests show that the RING-H2 domain is the key determinant of oligomerization. Mutational analysis suggests that the leucine-rich domain limits the accessibility of the RING-H2 domain and inhibits export and recruitment in addition to promoting Ste11 association and activation. Our results suggest that the major form of Ste5 is an inactive monomer with an inaccessible RING-H2 domain and Ste11 binding site, whereas the active form is an oligomer that is more efficiently exported and recruited and has a more accessible RING-H2 domain and Ste11 binding site.

scholarly journals F-actin binds to the cytoplasmic surface of ponticulin, a 17-kD integral glycoprotein from Dictyostelium discoideum plasma membranes.

1987 ◽  
Vol 105 (4) ◽  
pp. 1741-1751 ◽  
Author(s):  
L J Wuestehube ◽  
E J Luna
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Dictyostelium Discoideum ◽  
Plasma Membranes ◽  
Membrane Binding ◽  
Binding Activity ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Cytoplasmic Surface ◽  
Actin Binding Site

F-actin affinity chromatography and immunological techniques are used to identify actin-binding proteins in purified Dictyostelium discoideum plasma membranes. A 17-kD integral glycoprotein (gp17) consistently elutes from F-actin columns as the major actin-binding protein under a variety of experimental conditions. The actin-binding activity of gp17 is identical to that of intact plasma membranes: it resists extraction with 0.1 N NaOH, 1 mM dithiothreitol (DTT); it is sensitive to ionic conditions; it is stable over a wide range of pH; and it is eliminated by proteolysis, denaturation with heat, or treatment with DTT and N-ethylmaleimide. gp17 may be responsible for much of the actin-binding activity of plasma membranes since monovalent antibody fragments (Fab) directed primarily against gp17 inhibit actin-membrane binding by 96% in sedimentation assays. In contrast, Fab directed against cell surface determinants inhibit binding by only 0-10%. The actin-binding site of gp17 appears to be located on the cytoplasmic surface of the membrane since Fab against this protein continue to inhibit 96% of actin-membrane binding even after extensive adsorption against cell surfaces. gp17 is abundant in the plasma membrane, constituting 0.4-1.0% of the total membrane protein. A transmembrane orientation of gp17 is suggested since, in addition to the cytoplasmic localization of the actin-binding site, extracellular determinants of gp17 are identified. gp17 is surface-labeled by sulfo-N-hydroxy-succinimido-biotin, a reagent that cannot penetrate the cell membrane. Also, gp17 is glycosylated since it is specifically bound by the lectin, concanavalin A. We propose that gp17 is a major actin-binding protein that is important for connecting the plasma membrane to the underlying microfilament network. Therefore, we have named this protein "ponticulin" from the Latin word, ponticulus, which means small bridge.

Sign in / Sign up

Export Citation Format

Share Document