Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism - PubMed (original) (raw)
Review
. 2001 Oct 12;506(3):173-9.
doi: 10.1016/s0014-5793(01)02909-x.
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- PMID: 11602240
- DOI: 10.1016/s0014-5793(01)02909-x
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Review
Specificity in pleckstrin homology (PH) domain membrane targeting: a role for a phosphoinositide-protein co-operative mechanism
T Maffucci et al. FEBS Lett. 2001.
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Abstract
Pleckstrin homology (PH) domains are protein modules found in proteins involved in many cellular processes. The majority of PH domain-containing proteins require membrane association for their function. It has been shown that most PH domains interact directly with the cell membrane by binding to phosphoinositides with a broad range of specificity and affinity. While a highly specific binding of the PH domain to a phosphoinositide can be necessary and sufficient for the correct recruitment of the host protein to the membrane, a weaker and less specific interaction may be necessary but not sufficient, thus probably requiring alternative, co-operative mechanisms.
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