Copy Link
Add to Bookmark
Report

dictyNews Volume 43 Number 18

eZine's profile picture
Published in 
Dicty News
 · 10 months ago

dictyNews 
Electronic Edition
Volume 43, number 18
August 11, 2017

Please submit abstracts of your papers as soon as they have been
accepted for publication by sending them to dicty@northwestern.edu
or by using the form at
http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit.

Back issues of dictyNews, the Dicty Reference database and other
useful information is available at dictyBase - http://dictybase.org.

Follow dictyBase on twitter:
http://twitter.com/dictybase


=========
Abstracts
=========

The F-actin-binding RapGEF GflB is required for efficient macropinocytosis
in Dictyostelium

Hironori Inaba1,2,3, Koji Yoda1, Hiroyuki Adachi1

1Department of Biotechnology, Graduate School of Agricultural and Life
Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan
2Department of Cell Biology and 3The Center for Brain Integration Research,
Graduate School of Medical and Dental Science, Tokyo Medical and Dental
University, Bunkyo-ku, Tokyo 113-8510, Japan


J. Cell Sci., in press

Macropinocytosis involves the uptake of large volumes of fluid, which is
regulated by various small GTPases. The Dictyostelium discoideum protein
GflB is a guanine nucleotide exchange factor (GEF) of Rap1, involved in
chemotaxis. Here we studied the role of GflB in macropinocytosis,
phagocytosis, and cytokinesis. In plate culture of vegetative cells, compared
with the parental strain AX2, gflB KO cells were flatter and more polarized,
whereas GflB-overproducing cells were rounder. The gflB KO cells exhibited
impaired crown formation and retraction, particularly retraction, resulting in
more crowns (macropinocytic cups) per cell and longer crown lifetimes.
Accordingly, gflB KO cells showed defects in macropinocytosis and also in
phagocytosis and cytokinesis. F-actin was elevated in gflB KO cells. GflB
localized to the actin cortex especially at crowns and phagocytic cups. The
villin headpiece domain (VHP)-like N-terminal domain of GflB directly
interacted with F-actin in vitro. Furthermore, a domain enriched in basic
amino acids interacted with specific membrane cortex structures such as the
cleavage furrow. In conclusion, GflB acts as a key local regulator of actin-
driven membrane protrusion possibly by modulating Rap1 signaling pathways.


submitted by: Hiroyuki Adachi [adachih@mail.ecc.u-tokyo.ac.jp
==============================================================
[End dictyNews, volume 43, number 18]

← previous
next →
loading
sending ...
New to Neperos ? Sign Up for free
download Neperos App from Google Play
install Neperos as PWA

Let's discover also

Recent Articles

Recent Comments

Neperos cookies
This website uses cookies to store your preferences and improve the service. Cookies authorization will allow me and / or my partners to process personal data such as browsing behaviour.

By pressing OK you agree to the Terms of Service and acknowledge the Privacy Policy

By pressing REJECT you will be able to continue to use Neperos (like read articles or write comments) but some important cookies will not be set. This may affect certain features and functions of the platform.
OK
REJECT