These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: In vitro binding studies suggest a membrane-associated complex between erythroid p55, protein 4.1, and glycophorin C.
    Author: Marfatia SM, Lue RA, Branton D, Chishti AH.
    Journal: J Biol Chem; 1994 Mar 25; 269(12):8631-4. PubMed ID: 8132590.
    Abstract:
    p55 is a palmitoylated peripheral membrane phosphoprotein of human erythrocytes. Primary structure of p55 includes a single copy of the SH3 motif, a COOH-terminal guanylate kinase domain, and an NH2-terminal domain of unknown function. Although the function of p55 is not known, interest in this component has been heightened by its similarity to the Drosophila tumor suppressor discs-large (dlg). In this report we provide evidence for the direct association of p55 with the NH2-terminal 30-kDa domain of protein 4.1, a key component of the erythroid membrane skeleton. In addition, p55 also binds to the cytoplasmic domain of glycophorin C, a transmembrane protein of red blood cells. We also provide evidence demonstrating the direct association of the 30-kDa domain of protein 4.1 with the cytoplasmic domain of glycophorin C. Taken together, these results suggest the existence of a novel ternary complex at the erythroid plasma membrane involving protein 4.1, p55, and glycophorin C. Since isoforms of protein 4.1, p55, and glycophorin C are present in many non-erythroid cells, the binding interactions may be prototypical of similar associations that modulate cytoskeletal-membrane linkage of broad significance.
    [Abstract] [Full Text] [Related] [New Search]