Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins - PubMed (original) (raw)
. 2006 May 9;45(18):5725-32.
doi: 10.1021/bi060015v.
Affiliations
- PMID: 16669616
- DOI: 10.1021/bi060015v
Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins
Xiuli An et al. Biochemistry. 2006.
Abstract
Human erythrocyte protein 4.1 (4.1R) participates in organizing the plasma membrane by linking several surface-exposed transmembrane proteins to the internal cytoskeleton. In the present study, we characterized the interaction of 4.1R with phosphatidylinositol-4,5-bisphosphate (PIP2) and assessed the effect of PIP2 on the interaction of 4.1R with membrane proteins. We found that 4.1R bound to PIP2-containing liposomes through its N-terminal 30 kDa membrane-binding domain and PIP2 binding induced a conformational change in this domain. Phosphatidylinositol-4-phosphate (PIP) was a less effective inducer of this conformational change, and phosphatidylinositol (PI) and inositol-1,4,5-phosphate (IP3) induced no change. Replacement of amino acids K63,64 and K265,266 by alanine abolished the interaction of the membrane-binding domain with PIP2. Importantly, binding of PIP2 to 4.1R selectively modulated the ability of 4.1R to interact with its different binding partners. While PIP2 significantly enhanced the binding of 4.1R to glycophorin C (GPC), it inhibited the binding of 4.1R to band 3 in vitro. PIP2 had no effect on 4.1R binding to p55. Furthermore, GPC was more readily extracted by Triton X-100 from adenosine triphosphate (ATP)-depleted erythrocytes, implying that the GPC-4.1R interaction may be regulated by PIP2 in situ. These findings define an important role for PIP2 in regulating the function of 4.1R. Because 4.1R and its family members (4.1R, 4.1B, 4.1G, and 4.1N) are widely expressed and the PIP2-binding motifs are highly conserved, it is likely that the functions of other 4.1 proteins are similarly regulated by PIP2 in many different cell types.
Similar articles
- Marked difference in membrane-protein-binding properties of the two isoforms of protein 4.1R expressed at early and late stages of erythroid differentiation.
Nunomura W, Parra M, Hebiguchi M, Sawada K, Mohandas N, Takakuwa Y. Nunomura W, et al. Biochem J. 2009 Jan 1;417(1):141-8. doi: 10.1042/BJ20081372. Biochem J. 2009. PMID: 18691159 - Secretory carrier membrane protein SCAMP2 and phosphatidylinositol 4,5-bisphosphate interactions in the regulation of dense core vesicle exocytosis.
Liao H, Ellena J, Liu L, Szabo G, Cafiso D, Castle D. Liao H, et al. Biochemistry. 2007 Sep 25;46(38):10909-20. doi: 10.1021/bi701121j. Epub 2007 Aug 22. Biochemistry. 2007. PMID: 17713930 - Activation of inwardly rectifying potassium (Kir) channels by phosphatidylinosital-4,5-bisphosphate (PIP2): interaction with other regulatory ligands.
Xie LH, John SA, Ribalet B, Weiss JN. Xie LH, et al. Prog Biophys Mol Biol. 2007 Jul;94(3):320-35. doi: 10.1016/j.pbiomolbio.2006.04.001. Epub 2006 Jun 19. Prog Biophys Mol Biol. 2007. PMID: 16837026 Review. - Protein 4.1 and the control of ion channels.
Baines AJ, Bennett PM, Carter EW, Terracciano C. Baines AJ, et al. Blood Cells Mol Dis. 2009 May-Jun;42(3):211-5. doi: 10.1016/j.bcmd.2009.01.016. Epub 2009 Mar 9. Blood Cells Mol Dis. 2009. PMID: 19272819 Review.
Cited by
- Transparent Touch: Insights From Model Systems on Epidermal Control of Somatosensory Innervation.
Yin C, Peterman E, Rasmussen JP, Parrish JZ. Yin C, et al. Front Cell Neurosci. 2021 May 31;15:680345. doi: 10.3389/fncel.2021.680345. eCollection 2021. Front Cell Neurosci. 2021. PMID: 34135734 Free PMC article. Review. - Interaction of the human erythrocyte Band 3 anion exchanger 1 (AE1, SLC4A1) with lipids and glycophorin A: Molecular organization of the Wright (Wr) blood group antigen.
Kalli AC, Reithmeier RAF. Kalli AC, et al. PLoS Comput Biol. 2018 Jul 16;14(7):e1006284. doi: 10.1371/journal.pcbi.1006284. eCollection 2018 Jul. PLoS Comput Biol. 2018. PMID: 30011272 Free PMC article. - Characterization of ENU-induced Mutations in Red Blood Cell Structural Proteins.
Kildey K, Flower RL, Tran TV, Tunningley R, Harris J, Dean MM. Kildey K, et al. Comput Struct Biotechnol J. 2013 Sep 23;6:e201303012. doi: 10.5936/csbj.201303012. eCollection 2013. Comput Struct Biotechnol J. 2013. PMID: 24688720 Free PMC article. - A conserved function in phosphatidylinositol metabolism for mammalian Vps13 family proteins.
Park JS, Halegoua S, Kishida S, Neiman AM. Park JS, et al. PLoS One. 2015 Apr 27;10(4):e0124836. doi: 10.1371/journal.pone.0124836. eCollection 2015. PLoS One. 2015. PMID: 25915401 Free PMC article. - Protein 4.1R self-association: identification of the binding domain.
Pérez-Ferreiro CM, Lospitao E, Correas I. Pérez-Ferreiro CM, et al. Biochem J. 2006 Dec 15;400(3):457-65. doi: 10.1042/BJ20060644. Biochem J. 2006. PMID: 16881872 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
Miscellaneous