Phosphatidylserine specific binding protein in rat brain: Purification and characterization

Takashi Nakaoka; Naoya Kojima; Toshiro Hamamoto; Nobuyuki Kurosawa; Young Choon Lee; Hiroshi Kawasaki; Koichi Suzuki; Shuichi Tsuji

doi:10.1093/oxfordjournals.jbchem.a124196

Phosphatidylserine specific binding protein in rat brain: Purification and characterization

Takashi Nakaoka, Naoya Kojima, Toshiro Hamamoto, Nobuyuki Kurosawa, Young Choon Lee, Hiroshi Kawasaki, Koichi Suzuki, Shuichi Tsuji^*

^*Corresponding author for this work

Life Sciences and Bioengineering

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

A calcium-independent phosphatidylserine specific binding protein detected on liposome blotting analysis was purified from rat brain and revealed to be identical to myristoylated, alanine-rich C kinase substrate (MARCKS). MARCKS specifically binds to phosphatidylserine but not phosphatidylcholine. The binding of MARCKS to phosphatidylserine was abolished on protein kinase C-dependent phosphorylation. Since bacterially expressed MARCKS also specifically binds to phosphatidylserine, muristoylation of the N-terminal glycine seems not to be essential for the binding of MARCKS to phosphatidylserine. These data suggest that phosphatidylserine is a membranous target molecule of MARCKS.

Original language	English
Pages (from-to)	449-452
Number of pages	4
Journal	Journal of Biochemistry
Volume	114
Issue number	4
DOIs	https://doi.org/10.1093/oxfordjournals.jbchem.a124196
State	Published - 1993/10

ASJC Scopus subject areas

General Medicine

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title = "Phosphatidylserine specific binding protein in rat brain: Purification and characterization",

abstract = "A calcium-independent phosphatidylserine specific binding protein detected on liposome blotting analysis was purified from rat brain and revealed to be identical to myristoylated, alanine-rich C kinase substrate (MARCKS). MARCKS specifically binds to phosphatidylserine but not phosphatidylcholine. The binding of MARCKS to phosphatidylserine was abolished on protein kinase C-dependent phosphorylation. Since bacterially expressed MARCKS also specifically binds to phosphatidylserine, muristoylation of the N-terminal glycine seems not to be essential for the binding of MARCKS to phosphatidylserine. These data suggest that phosphatidylserine is a membranous target molecule of MARCKS.",

author = "Takashi Nakaoka and Naoya Kojima and Toshiro Hamamoto and Nobuyuki Kurosawa and Lee, {Young Choon} and Hiroshi Kawasaki and Koichi Suzuki and Shuichi Tsuji",

year = "1993",

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doi = "10.1093/oxfordjournals.jbchem.a124196",

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T1 - Phosphatidylserine specific binding protein in rat brain

T2 - Purification and characterization

AU - Nakaoka, Takashi

AU - Kojima, Naoya

AU - Hamamoto, Toshiro

AU - Kurosawa, Nobuyuki

AU - Lee, Young Choon

AU - Kawasaki, Hiroshi

AU - Suzuki, Koichi

AU - Tsuji, Shuichi

PY - 1993/10

Y1 - 1993/10

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AB - A calcium-independent phosphatidylserine specific binding protein detected on liposome blotting analysis was purified from rat brain and revealed to be identical to myristoylated, alanine-rich C kinase substrate (MARCKS). MARCKS specifically binds to phosphatidylserine but not phosphatidylcholine. The binding of MARCKS to phosphatidylserine was abolished on protein kinase C-dependent phosphorylation. Since bacterially expressed MARCKS also specifically binds to phosphatidylserine, muristoylation of the N-terminal glycine seems not to be essential for the binding of MARCKS to phosphatidylserine. These data suggest that phosphatidylserine is a membranous target molecule of MARCKS.

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Phosphatidylserine specific binding protein in rat brain: Purification and characterization

Abstract

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