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Rap1 is a small GTPase that modulates adhesion of T cells by regulating inside-out signaling through LFA-1. The bulk of Rap1 is expressed in a GDP-bound state on intracellular vesicles. Exocytosis of these vesicles delivers Rap1 to the plasma membrane, where it becomes activated. We report here that phospholipase D1 (PLD1) is expressed on the same vesicular compartment in T cells as Rap1 and is translocated to the plasma membrane along with Rap1. Moreover, PLD activity is required for both translocation and activation of Rap1. Increased T-cell adhesion in response to stimulation of the antigen receptor depended on PLD1. C3G, a Rap1 guanine nucleotide exchange factor located in the cytosol of resting cells, translocated to the plasma membranes of stimulated T cells. Our data support a model whereby PLD1 regulates Rap1 activity by controlling exocytosis of a stored, vesicular pool of Rap1 that can be activated by C3G upon delivery to the plasma membrane.

Original publication

DOI

10.1128/mcb.00366-09

Type

Journal article

Journal

Molecular and cellular biology

Publication Date

06/2009

Volume

29

Pages

3297 - 3306

Addresses

The Cancer Institute, NYU School of Medicine, New York, New York 10016, USA.

Keywords

T-Lymphocytes, COS Cells, Hela Cells, Jurkat Cells, Cell Membrane, Cytoplasmic Vesicles, Animals, Mice, Inbred C57BL, Cercopithecus aethiops, Humans, Mice, rap1 GTP-Binding Proteins, Phospholipase D, Guanine Nucleotide-Releasing Factor 2, Recombinant Proteins, Cell Adhesion, Up-Regulation, Biological Transport, Active, Models, Biological, Female, In Vitro Techniques