The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions.
Eukaryotic cells extend a variety of surface protrusions to direct cell motility. Formation of protrusions is mediated by coordinated actions between the plasma membrane and the underlying actin cytoskeleton. Here, we found that the single calponin homology (CH) domain-containing protein CHDP-1 indu...
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2016-07-01
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doaj-ff274b816604469fb84fe2d8de63a2162020-11-25T00:07:15ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042016-07-01127e100616310.1371/journal.pgen.1006163The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions.Liying GuanXuehua MaJingyan ZhangJia-Jia LiuYingchun WangMei DingEukaryotic cells extend a variety of surface protrusions to direct cell motility. Formation of protrusions is mediated by coordinated actions between the plasma membrane and the underlying actin cytoskeleton. Here, we found that the single calponin homology (CH) domain-containing protein CHDP-1 induces the formation of cell protrusions in C. elegans. CHDP-1 is anchored to the cortex through its amphipathic helix. CHDP-1 associates through its CH domain with the small GTPase Rac1/CED-10, which is a key regulator of the actin cytoskeleton. CHDP-1 preferentially binds to the GTP-bound active form of the CED-10 protein and preserves the membrane localization of GTP-CED-10. Hence, by coupling membrane expansion to Rac1-mediated actin dynamics, CHDP-1 promotes the formation of cellular protrusions in vivo.http://europepmc.org/articles/PMC4944944?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Liying Guan Xuehua Ma Jingyan Zhang Jia-Jia Liu Yingchun Wang Mei Ding |
spellingShingle |
Liying Guan Xuehua Ma Jingyan Zhang Jia-Jia Liu Yingchun Wang Mei Ding The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. PLoS Genetics |
author_facet |
Liying Guan Xuehua Ma Jingyan Zhang Jia-Jia Liu Yingchun Wang Mei Ding |
author_sort |
Liying Guan |
title |
The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. |
title_short |
The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. |
title_full |
The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. |
title_fullStr |
The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. |
title_full_unstemmed |
The Calponin Family Member CHDP-1 Interacts with Rac/CED-10 to Promote Cell Protrusions. |
title_sort |
calponin family member chdp-1 interacts with rac/ced-10 to promote cell protrusions. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS Genetics |
issn |
1553-7390 1553-7404 |
publishDate |
2016-07-01 |
description |
Eukaryotic cells extend a variety of surface protrusions to direct cell motility. Formation of protrusions is mediated by coordinated actions between the plasma membrane and the underlying actin cytoskeleton. Here, we found that the single calponin homology (CH) domain-containing protein CHDP-1 induces the formation of cell protrusions in C. elegans. CHDP-1 is anchored to the cortex through its amphipathic helix. CHDP-1 associates through its CH domain with the small GTPase Rac1/CED-10, which is a key regulator of the actin cytoskeleton. CHDP-1 preferentially binds to the GTP-bound active form of the CED-10 protein and preserves the membrane localization of GTP-CED-10. Hence, by coupling membrane expansion to Rac1-mediated actin dynamics, CHDP-1 promotes the formation of cellular protrusions in vivo. |
url |
http://europepmc.org/articles/PMC4944944?pdf=render |
work_keys_str_mv |
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