Structural basis for high-affinity phosphoinositide binding by pleckstrin homology domains

1999 ◽  
Vol 27 (4) ◽  
pp. 617-624 ◽  
Author(s):  
M. A. Lemmon
Keyword(s):  
Structural Basis ◽  
Pleckstrin Homology ◽  
High Affinity ◽  
Homology Domains

scholarly journals Structural Basis for Discrimination of 3-Phosphoinositides by Pleckstrin Homology Domains

2000 ◽  
Vol 6 (2) ◽  
pp. 373-384 ◽  
Author(s):  
Kathryn M. Ferguson ◽  
Jennifer M. Kavran ◽  
Vijay G. Sankaran ◽  
Emmanuel Fournier ◽  
Steven J. Isakoff ◽  
...  
Keyword(s):  
Structural Basis ◽  
Pleckstrin Homology ◽  
Homology Domains

scholarly journals Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains

EMBO Reports ◽  
2010 ◽  
Vol 11 (4) ◽  
pp. 279-284 ◽  
Author(s):  
Marc Lenoir ◽  
Ünal Coskun ◽  
Michal Grzybek ◽  
Xinwang Cao ◽  
Sabine B Buschhorn ◽  
...  
Keyword(s):  
Structural Basis ◽  
Golgi Membrane ◽  
Pleckstrin Homology ◽  
Homology Domains

scholarly journals The Pleckstrin Homology Domains of Dynamin Isoforms Require Oligomerization for High Affinity Phosphoinositide Binding

1998 ◽  
Vol 273 (42) ◽  
pp. 27725-27733 ◽  
Author(s):  
Daryl E. Klein ◽  
Anthony Lee ◽  
David W. Frank ◽  
Michael S. Marks ◽  
Mark A. Lemmon
Keyword(s):  
Pleckstrin Homology ◽  
High Affinity ◽  
Homology Domains

scholarly journals Pleckstrin homology (PH) domains and phosphoinositides

2007 ◽  
Vol 74 ◽  
pp. 81-93 ◽  
Author(s):  
Mark A. Lemmon
Keyword(s):  
Ph Domain ◽  
Pleckstrin Homology ◽  
High Affinity ◽  
Weak Binding ◽  
Ph Domains ◽  
Common Domain ◽  
Functional Relevance ◽  
Phox Homology ◽  
Adp Ribosylation Factor ◽  
Homology Domains

PH (pleckstrin homology) domains represent the 11th most common domain in the human proteome. They are best known for their ability to bind phosphoinositides with high affinity and specificity, although it is now clear that less than 10% of all PH domains share this property. Cases in which PH domains bind specific phosphoinositides with high affinity are restricted to those phosphoinositides that have a pair of adjacent phosphates in their inositol headgroup. Those that do not [PtdIns3P, PtdIns5P and PtdIns(3,5)P2] are instead recognized by distinct classes of domains including FYVE domains, PX (phox homology) domains, PHD (plant homeodomain) fingers and the recently identified PROPPINs (b-propellers that bind polyphosphoinositides). Of the 90% of PH domains that do not bind strongly and specifically to phosphoinositides, few are well understood. One group of PH domains appears to bind both phosphoinositides (with little specificity) and Arf (ADP-ribosylation factor) family small G-proteins, and are targeted to the Golgi apparatus where both phosphoinositides and the relevant Arfs are both present. Here, the PH domains may function as coincidence detectors. A central challenge in understanding the majority of PH domains is to establish whether the very low affinity phosphoinositide binding reported in many cases has any functional relevance. For PH domains from dynamin and from Dbl family proteins, this weak binding does appear to be functionally important, although its precise mechanistic role is unclear. In many other cases, it is quite likely that alternative binding partners are more relevant, and that the observed PH domain homology represents conservation of structural fold rather than function.

Molecular determinants in pleckstrin homology domains that allow specific recognition of phosphoinositides

2001 ◽  
Vol 29 (4) ◽  
pp. 377-384 ◽  
Author(s):  
M. A. Lemmon ◽  
K. M. Ferguson
Keyword(s):  
Binding Sites ◽  
Human Proteome ◽  
Specific Interactions ◽  
Structural Studies ◽  
Pleckstrin Homology ◽  
High Affinity ◽  
Specific Recognition ◽  
Molecular Determinants ◽  
Ph Domains ◽  
Homology Domains

More than 250 pleckstrin homology (PH) domains have been identified in the human proteome. All PH domains studied to date appear to bind phosphoinositides, most binding only weakly and non-specifically. Members of a small subclass of PH domains show both high affinity and specificity for particular phosphoinositides, and recent structural studies have provided detailed views of these specific interactions. We discuss the architecture of the specific phosphoinositide-binding sites of PH domains, and how selectivity can be modulated by sequence changes.

scholarly journals Structural Basis of 3-Phosphoinositide Recognition by Pleckstrin Homology Domains

2000 ◽  
Vol 6 (2) ◽  
pp. 385-394 ◽  
Author(s):  
Susan E. Lietzke ◽  
Sahana Bose ◽  
Thomas Cronin ◽  
Jes Klarlund ◽  
Anil Chawla ◽  
...  
Keyword(s):  
Structural Basis ◽  
Pleckstrin Homology ◽  
Phosphoinositide Recognition ◽  
Homology Domains

scholarly journals The structural basis for high‐affinity uptake of lignin‐derived aromatic compounds by proteobacterial TRAP transporters

FEBS Journal ◽  
2021 ◽  
Author(s):  
Claudine Bisson ◽  
Robert C. Salmon ◽  
Laura West ◽  
John B. Rafferty ◽  
Andrew Hitchcock ◽  
...  
Keyword(s):  
Aromatic Compounds ◽  
Structural Basis ◽  
High Affinity ◽  
High Affinity Uptake

Pleckstrin homology domains: not just for phosphoinositides

2004 ◽  
Vol 32 (5) ◽  
pp. 707-711 ◽  
Author(s):  
M.A. Lemmon
Keyword(s):  
Subcellular Localization ◽  
Human Genome ◽  
Small Gtpases ◽  
Membrane Targeting ◽  
Ph Domain ◽  
Cellular Membranes ◽  
Pleckstrin Homology ◽  
Ph Domains ◽  
Common Domain ◽  
Homology Domains

PH domains (pleckstrin homology domains) are the 11th most common domain in the human genome and are best known for their ability to target cellular membranes by binding specifically to phosphoinositides. Recent studies in yeast have shown that, in fact, this is a property of only a small fraction of the known PH domains. Most PH domains are not capable of independent membrane targeting, and those capable of doing so (approx. 33%) appear, most often, to require both phosphoinositide and non-phosphoinositide determinants for their subcellular localization. Several recent studies have suggested that small GTPases such as ARF family proteins play a role in defining PH domain localization. Some others have described a signalling role for PH domains in regulating small GTPases, although phosphoinositides may also play a role. These findings herald a change in our perspective of PH domain function, which will be significantly more diverse than previously supposed.

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