p95-APP1 links membrane transport to Rac-mediated reorganization of actin

被引：108

作者：

Di Cesare, A

Paris, S

Albertinazzi, C

Dariozzi, S

Andersen, J

Mann, M

Longhi, R

de Curtis, I

机构：

[1] Ist Sci San Raffaele, DIBIT, Cell Adhes Unit, I-20132 Milan, Italy

[2] Odense Univ, Ctr Expt Bioinformat, DK-5230 Odense M, Denmark

[3] CNR, Inst Biocatalysis & Mol Recognit, I-20133 Milan, Italy

来源：

NATURE CELL BIOLOGY | 2000年 / 2卷 / 08期

关键词：

D O I：

10.1038/35019561

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Motility requires protrusive activity at the cellular edge, where Rho family members regulate actin dynamics. Here we show that p95-APP1 (ArfGAP-putative, Pix-interacting, paxillin-interacting protein 1), a member of the GIT1/PKL family, is part of a complex that interacts with pac. Wild-type and truncated p95-APP1 induce actin-rich protrusions mediated by Rac and ADP-ribosylation factor 6 (Arf6). Distinct p95-APP1-derived polypeptides have different distributions, indicating that p95-APP1 cycles between the cell surface and endosomes. Our results show that p95-APP1 functionally interacts with pac and localizes to endosomal compartments, thus identifying p95-APP1 as a molecular link between actin organization, adhesion, and membrane transport during cell motility.

引用

页码：521 / 530

页数：10

共 46 条

[21] CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].