scholarly journals Replacements of Single Basic Amino Acids in the Pleckstrin Homology Domain of Phospholipase C-δ1 Alter the Ligand Binding, Phospholipase Activity, and Interaction with the Plasma Membrane

1998 ◽  
Vol 273 (1) ◽  
pp. 417-424 ◽  
Author(s):  
Hitoshi Yagisawa ◽  
Kaori Sakuma ◽  
Hugh F. Paterson ◽  
Robert Cheung ◽  
Victoria Allen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Ligand Binding ◽  
Phospholipase C ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Phospholipase Activity ◽  
Basic Amino Acids

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 Carboxyl-terminal basic amino acids in the X domain are essential for the nuclear import of phospholipase C δ1

2002 ◽  
Vol 7 (9) ◽  
pp. 985-996 ◽  
Author(s):  
Masashi Okada ◽  
Makoto Fujii ◽  
Masaki Yamaga ◽  
Hiroaki Sugimoto ◽  
Hiroyuki Sadano ◽  
...  
Keyword(s):  
Amino Acids ◽  
Phospholipase C ◽  
Nuclear Import ◽  
Basic Amino Acids ◽  
Carboxyl Terminal

scholarly journals Interaction of Elongation Factor-1α and Pleckstrin Homology Domain of Phospholipase C-γ1 with Activating Its Activity

2002 ◽  
Vol 277 (22) ◽  
pp. 19697-19702 ◽  
Author(s):  
Jong-Soo Chang ◽  
Heon Seok ◽  
Taeg-Kyu Kwon ◽  
Do Sik Min ◽  
Bong-Hyun Ahn ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Elongation Factor ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Elongation Factor 1Α

scholarly journals Influence of membrane curvature on the structure of the membrane-associated pleckstrin homology domain of phospholipase C-δ1

2009 ◽  
Vol 1788 (12) ◽  
pp. 2575-2583 ◽  
Author(s):  
Naoko Uekama ◽  
Takahiro Aoki ◽  
Toshihiro Maruoka ◽  
Seiji Kurisu ◽  
Akiko Hatakeyama ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Membrane Curvature ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology

scholarly journals Basic Residues in the Mason-Pfizer Monkey Virus Gag Matrix Domain Regulate Intracellular Trafficking and Capsid-Membrane Interactions

2007 ◽  
Vol 81 (17) ◽  
pp. 8977-8988 ◽  
Author(s):  
Elizabeth Stansell ◽  
Robert Apkarian ◽  
Sarka Haubova ◽  
William E. Diehl ◽  
Ewan M. Tytler ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Intracellular Transport ◽  
Wild Type ◽  
Membrane Interactions ◽  
Cortical Actin ◽  
Basic Amino Acids ◽  
Gag Polyprotein ◽  
The Matrix ◽  
Arginine Residues

ABSTRACT Mason-Pfizer monkey virus (M-PMV) capsids that have assembled in the cytoplasm must be transported to and associate with the plasma membrane prior to being enveloped by a lipid bilayer during viral release. Structural studies have identified a positive-charge density on the membrane-proximal surface of the matrix (MA) protein component of the Gag polyprotein. To investigate if basic amino acids in MA play a role in intracellular transport and capsid-membrane interactions, mutants were constructed in which lysine and arginine residues (R10, K16, K20, R22, K25, K27, K33, and K39) potentially exposed on the capsid surface were replaced singly and in pairs by alanine. A majority of the charge substitution mutants were released less efficiently than the wild type. Electron microscopy of mutant Gag-expressing cells revealed four distinct phenotypes: K16A and K20A immature capsids accumulated on and budded into intracellular vesicles; R10A, K27A, and R22A capsid transport was arrested at the cellular cortical actin network, while K25A immature capsids were dispersed throughout the cytoplasm and appeared to be defective at an earlier stage of intracellular transport; and the remaining mutant (K33A and K39A) capsids accumulated at the inner surface of the plasma membrane. All mutants that released virions exhibited near-wild-type infectivity in a single-round assay. Thus, basic amino acids in the M-PMV MA define both cellular location and efficiency of virus release.

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