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Title
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Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate.
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Authors
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J.E.Harlan,
P.J.Hajduk,
H.S.Yoon,
S.W.Fesik.
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Ref.
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Nature, 1994,
371,
168-170.
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PubMed id
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Abstract
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The pleckstrin homology (PH) domain is a new protein module of around 100 amino
acids found in several proteins involved in signal transduction. Although its
specific function has yet to be elucidated, the carboxy-terminal regions of many
PH domains bind to the beta gamma subunits of G proteins. On the basis of
structural similarities between PH domains and lipid-binding proteins, we have
proposed that PH domains may be binding to lipophilic molecules. Indeed, many of
the proteins that contain this domain associate with phospholipid membranes, and
disruption of this domain can interfere with membrane association. Here we
report that PH domains bind to phosphatidylinositol-4,5-bisphosphate and show
that the lipid-binding site is located at the lip of the beta-barrel. This
suggests that PH domains may be important for membrane localization of proteins
through interactions with phosphatidylinositol-4,5-bisphosphate.
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