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Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1

Jian, Xiaoying, Tang, Wai-Kwan, Zhai, Peng, Roy, Neeladri Sekhar, Luo, Ruibai, Gruschus, James M., Yohe, Marielle E., Chen, Pei-Wen, Li, Yifei, Byrd, R. Andrew, Xia, Di, Randazzo, Paul A.·2015·Structure
DOI 10.1016/j.str.2015.08.008PMC PMC4788500
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  • The PH domain of Arf GAP ASAP1 possesses two synergistic lipid-binding sites and binds most efficiently to PI(4,5)P2-containing membranes in the presence of other anionic lipids, such as PS.

    “For example, the PH domain of Arf GAP ASAP1 possesses two synergistic lipid‐binding sites and binds most efficiently to PI(4,5)P2‐containing membranes in the presence of other anionic lipids, such as PS (Jian et al, 2015).”

    From Molecular basis of accessible plasma membrane cholesterol recognition by the GRAM domain of GRAMD1b (2021) · cites this paper as Jian et al, 2015

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Metadata

Authors
Jian, X., Tang, W.-K., Zhai, P., Roy, N. S., Luo, R., Gruschus, J. M., Yohe, M. E., Chen, P.-W., Li, Y., Byrd, R. A., Xia, D., & Randazzo, P. A.
Venue
Structure
Publisher
Elsevier BV
Published
2015-11
Volume
23
Issue
11
Pages
1977-1988
ISSN
0969-2126
DOI
10.1016/j.str.2015.08.008
PMC
PMC4788500
Cited by
67
References
0
Language
en
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