Fluorescent indicators for inositol 1,4,5-trisphosphate based on bioconjugates of pleckstrin homology domain and fluorescent dyes

1999 ◽  
Vol 36 (5) ◽  
pp. 175-177 ◽  
Author(s):  
Kenzo Hirose ◽  
Hiroshi Takeshima ◽  
Masamitsu Iino ◽  
Kenzo Hirose ◽  
Hiroshi Takeshima ◽  
...  
Keyword(s):  
Fluorescent Dyes ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Fluorescent Indicators ◽  
Inositol 1,4,5 Trisphosphate

scholarly journals Phospholipase C δ1 requires a pleckstrin homology domain for interaction with the plasma membrane

1995 ◽  
Vol 312 (3) ◽  
pp. 661-666 ◽  
Author(s):  
H F Paterson ◽  
J W Savopoulos ◽  
O Perisic ◽  
R Cheung ◽  
M V Ellis ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Phospholipase C ◽  
Living Cells ◽  
Pleckstrin Homology Domain ◽  
Deletion Mutants ◽  
Pleckstrin Homology ◽  
Structural Requirements ◽  
Inositol 1,4,5 Trisphosphate ◽  
Membrane Attachment

The structural requirements of phospholipase C delta 1 for interaction with the plasma membrane were analysed by immunofluorescence after microinjection into living cells. Microinjection of deletion mutants revealed that the region required for membrane attachment and binding of inositol 1,4,5-trisphosphate in vitro corresponded to the pleckstrin homology domain, a structural module described in more than 90 proteins.

scholarly journals GαqDirectly Activates p63RhoGEF and Trio via a Conserved Extension of the Dbl Homology-associated Pleckstrin Homology Domain

2007 ◽  
Vol 282 (40) ◽  
pp. 29201-29210 ◽  
Author(s):  
Rafael J. Rojas ◽  
Marielle E. Yohe ◽  
Svetlana Gershburg ◽  
Takeharu Kawano ◽  
Tohru Kozasa ◽  
...  
Keyword(s):  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology

Structural Characterization of the Interaction between a Pleckstrin Homology Domain and Phosphatidylinositol 4,5-Bisphosphate

Biochemistry ◽  
1995 ◽  
Vol 34 (31) ◽  
pp. 9859-9864 ◽  
Author(s):  
John E. Harlan ◽  
Ho Sup Yoon ◽  
Philip J. Hajduk ◽  
Stephen W. Fesik
Keyword(s):  
Structural Characterization ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology

scholarly journals Critical Role for Kalirin in Nerve Growth Factor Signaling through TrkA

2005 ◽  
Vol 25 (12) ◽  
pp. 5106-5118 ◽  
Author(s):  
Kausik Chakrabarti ◽  
Rong Lin ◽  
Noraisha I. Schiller ◽  
Yanping Wang ◽  
David Koubi ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Pc12 Cells ◽  
Critical Role ◽  
Neuronal Morphology ◽  
Neurotrophin Receptor ◽  
General Mechanism ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Nerve Growth

ABSTRACT Kalirin is a multidomain guanine nucleotide exchange factor (GEF) that activates Rho proteins, inducing cytoskeletal rearrangement in neurons. Although much is known about the effects of Kalirin on Rho GTPases and neuronal morphology, little is known about the association of Kalirin with the receptor/signaling systems that affect neuronal morphology. Our experiments demonstrate that Kalirin binds to and colocalizes with the TrkA neurotrophin receptor in neurons. In PC12 cells, inhibition of Kalirin expression using antisense RNA decreased nerve growth factor (NGF)-induced TrkA autophosphorylation and process extension. Kalirin overexpression potentiated neurotrophin-stimulated TrkA autophosphorylation and neurite outgrowth in PC12 cells at a low concentration of NGF. Furthermore, elevated Kalirin expression resulted in catalytic activation of TrkA, as demonstrated by in vitro kinase assays and increased NGF-stimulated cellular activation of Rac, Mek, and CREB. Domain mapping demonstrated that the N-terminal Kalirin pleckstrin homology domain mediates the interaction with TrkA. The effects of Kalirin on TrkA provide a molecular basis for the requirement of Kalirin in process extension from PC12 cells and for previously observed effects on axonal extension and dendritic maintenance. The interaction of TrkA with the pleckstrin homology domain of Kalirin may be one example of a general mechanism whereby receptor/Rho GEF pairings play an important role in receptor tyrosine kinase activation and signal transduction.

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