Open AccessCentral role of PI 3K– SYK interaction in fibrinogen‐induced lamellipodia and filopodia formation in platelets
Author(s) -
Singh Raghvendra
Publication year - 2016
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12149
Subject(s) - lamellipodium , filopodia , microbiology and biotechnology , cdc42 , chemistry , syk , cytoskeleton , actin , biology , signal transduction , biochemistry , cell , tyrosine kinase
The WAVE complex‐1, a complex of WAVE , Abi1, NAP 1, PIR 121, HSPC 300, Rac GTP and Arp2/3 proteins, and WASP complex‐1, a complex of WASP , Cdc42, PIP 2, and Arp2/3 proteins, are involved in lamellipodia and filopodia formation, respectively. It is known that the two complexes have opposite dynamics. Furthermore, Rac has two guanine nucleotide exchange factors, Vav and Sos, whose role in activating Rac is not well understood. In this work, by the construction of signaling network, analysis, and mathematical modeling, I show that Sos generates a pulse of WAVE complex‐1, decreasing the response time of WAVE complex‐1 formation upon the stimulation of platelets by fibrinogen. Furthermore, I also show that the dynamics of WAVE and WASP complexes depends on PI 3K– SYK interaction. In the absence of this interaction, the WAVE complex‐1 does not form and the WASP complex‐1 remains at the initial, sustained level. Thus, I show the significance of the two protein/protein complexes: Sos and PI 3K– SYK interaction, in fibrinogen‐induced lamellipodia and filopodia formation in platelets.