Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin

被引：9

作者：

Goldmann, WH

机构：

[1] Harvard Univ, Sch Med, Childrens Hosp, Dept Pathol, Boston, MA 02115 USA

[2] Harvard Univ, Sch Med, Childrens Hosp, Dept Surg, Boston, MA 02115 USA

来源：

CELL BIOLOGY INTERNATIONAL | 2001年 / 25卷 / 08期

关键词：

tyrosine phosphorylation; filamin (ABP-280); actin; integrin; lipid membrane;

D O I：

10.1006/cbir.2000.0710

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Actin-binding protein (ABP-280: filamin) is a phosphoprotein present in the periphery of the cytoplasm, where it can cross-link actin filaments, associate with lipid membranes, and bind to membrane surface receptors. Given its function and localization in the cell, the hypothesis that it serves as a substrate for p56(lek), a lymphocyte-specific member of the src family of protein tyrosine kinases associated with cell surface glycoproteins is considered. The results suggest conformationally-induced regulation of filamin (ABP-280). (C) 2001 Academic Press.

引用

收藏

页码：805 / 808

页数：4

相关论文

共 23 条

[11] Filamin binds to the cytoplasmic domain of the β1-integrin -: Identification of amino acids responsible for this interaction [J].

Loo, DT ;

Kanner, SB ;

Aruffo, A .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (36) :23304-23312

[12] CYTOSKELETON PLASMA-MEMBRANE INTERACTIONS [J].

LUNA, EJ ;

HITT, AL .

SCIENCE, 1992, 258 (5084) :955-963

[13] Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells [J].

Marti, A ;

Luo, ZJ ;

Cunningham, C ;

Ohta, Y ;

Hartwig, J ;

Stossel, TP ;

Kyriakis, JM ;

Avruch, J .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (05) :2620-2628

[14] Signal transduction and glycophosphatidylinositol-linked proteins (LYN, LCK, CD4, CD45, G proteins, and CD55) selectively localize in triton-insoluble plasma membrane domains of human leukemic cell lines and normal granulocytes [J].

Parolini, I ;

Sargiacomo, M ;

Lisanti, MP ;

Peschle, C .

BLOOD, 1996, 87 (09) :3783-3794

[15]

Sharma CP, 1998, MOL BIOL CELL, V9, p17A

[16]

SHARMA CP, 1995, J IMMUNOL, V154, P3461

[17] INTERACTION OF THE 47-KDA TALIN FRAGMENT AND THE 32-KDA VINCULIN FRAGMENT WITH ACIDIC PHOSPHOLIPIDS - A COMPUTER-ANALYSIS [J].

TEMPEL, M ;

GOLDMANN, WH ;

ISENBERG, G ;

SACKMANN, E .

BIOPHYSICAL JOURNAL, 1995, 69 (01) :228-241

[18] COMPUTER ANALYSES SUGGEST INTERACTIONS OF NONMUSCLE FILAMIN WITH LIPID-MEMBRANES [J].

TEMPEL, M ;

GOLDMANN, WH ;

ISENBERG, G .

FEBS LETTERS, 1994, 350 (2-3) :169-172

[19] INSERTION OF FILAMIN INTO LIPID-MEMBRANES EXAMINED BY CALORIMETRY, THE FILM BALANCE TECHNIQUE, AND LIPID PHOTOLABELING [J].

TEMPEL, M ;

GOLDMANN, WH ;

DIETRICH, C ;

NIGGLI, V ;

WEBER, T ;

SACKMANN, E ;

ISENBERG, G .

BIOCHEMISTRY, 1994, 33 (42) :12565-12572

[20] INTERLEUKIN-2 REGULATES THE ACTIVITY OF THE LYN PROTEIN-TYROSINE KINASE IN A B-CELL LINE [J].

TORIGOE, T ;

SARAGOVI, HU ;

REED, JC .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (07) :2674-2678