Signal-dependent membrane targeting by pleckstrin homology (PH) domains.

By M. Lemmon, K. Ferguson. Biochemical Journal, 2000

725 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

The dynamin superfamily: universal membrane tubulation and fission molecules? (2004, neutral): “The affinity of a single PH domain for head groups is low (about 1 mM for inositol-1,4,5-trisphosphate) compared to other PH domain”
Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. (2002, background): “PH domains are known to bind to phosphorylated phosphoinositides (PIPs) as well as proteins (Rebecchi and Scarlata 1998; Lemmon and Ferguson 2000), and two possible functional roles have been suggested.”
The gene encoding alsin, a protein with three guanine-nucleotide exchange factor domains, is mutated in a form of recessive amyotrophic lateral sclerosis (2001, background): “Pleckstrin homology domains target their host proteins to membranes by binding to phophoinositides, and are involved in cell signaling and cytoskeletal rearrangement, among other thing”
PIP(2) and proteins: interactions, organization, and information flow. (2002, background): “The mechanism by which PLC δ-PH and several other PH domains bind phosphoinositides is revealed by crystal structures of the domains with bound IP3 (36, 65, 81).”
PDZ Domain Proteins: Plug and Play! (2003, background): “Second, all three domains have the ability to interact with peptides and lipids, albeit with different preferences (46, 47).”