Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain

Domenico De Rasmo; Giuseppe Palmisano; Salvatore Scacco; Zuzana Technikova-Dobrova; Damiano Panelli; Tiziana Cocco; Anna Maria Sardanelli; Antonio Gnoni; Loris Micelli; Antonio Trani; Aldo Di Luccia; Sergio Papa

doi:10.1016/j.mito.2010.04.005

Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain

Domenico De Rasmo, Giuseppe Palmisano, Salvatore Scacco, Zuzana Technikova-Dobrova, Damiano Panelli, Tiziana Cocco, Anna Maria Sardanelli, Antonio Gnoni, Loris Micelli, Antonio Trani, Aldo Di Luccia, Sergio Papa

Fondazione Santa Lucia

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

Abstract

The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS-PAGE electrophoresis, ³²P labelling and immunodetection show that " in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. ³²P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.

Original language	English
Pages (from-to)	464-471
Number of pages	8
Journal	Mitochondrion
Volume	10
Issue number	5
DOIs	https://doi.org/10.1016/j.mito.2010.04.005
Publication status	Published - Aug 2010

Keywords

CAMP-dependent protein kinase
Complex I
Mitochondrial phosphoproteins
NDUFS4 phosphorylation

ASJC Scopus subject areas

Cell Biology
Molecular Biology
Molecular Medicine

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10.1016/j.mito.2010.04.005

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title = "Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain",

abstract = "The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS-PAGE electrophoresis, 32P labelling and immunodetection show that {"} in vitro{"} PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. 32P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.",

keywords = "CAMP-dependent protein kinase, Complex I, Mitochondrial phosphoproteins, NDUFS4 phosphorylation",

author = "Rasmo, {Domenico De} and Giuseppe Palmisano and Salvatore Scacco and Zuzana Technikova-Dobrova and Damiano Panelli and Tiziana Cocco and Sardanelli, {Anna Maria} and Antonio Gnoni and Loris Micelli and Antonio Trani and Luccia, {Aldo Di} and Sergio Papa",

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month = aug,

doi = "10.1016/j.mito.2010.04.005",

language = "English",

volume = "10",

pages = "464--471",

journal = "Mitochondrion",

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TY - JOUR

T1 - Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain

AU - Rasmo, Domenico De

AU - Palmisano, Giuseppe

AU - Scacco, Salvatore

AU - Technikova-Dobrova, Zuzana

AU - Panelli, Damiano

AU - Cocco, Tiziana

AU - Sardanelli, Anna Maria

AU - Gnoni, Antonio

AU - Micelli, Loris

AU - Trani, Antonio

AU - Luccia, Aldo Di

AU - Papa, Sergio

PY - 2010/8

Y1 - 2010/8

N2 - The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS-PAGE electrophoresis, 32P labelling and immunodetection show that " in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. 32P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.

AB - The NDUFS4 subunit of complex I of the mammalian respiratory chain has a fully conserved carboxy-terminus with a canonical RVSTK phosphorylation site. Immunochemical analysis with specific antibodies shows that the serine in this site of the protein is natively present in complex I in both the phosphorylated and non-phosphorylated state. Two-dimensional IEF/SDS-PAGE electrophoresis, 32P labelling and immunodetection show that " in vitro" PKA phosphorylates the serine in the C-terminus of the NDUFS4 subunit in isolated bovine complex I. 32P labelling and TLC phosphoaminoacid mapping show that PKA phosphorylates serine and threonine residues in the purified heterologous human NDUFS4 protein.

KW - CAMP-dependent protein kinase

KW - Complex I

KW - Mitochondrial phosphoproteins

KW - NDUFS4 phosphorylation

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DO - 10.1016/j.mito.2010.04.005

M3 - Article

C2 - 20433953

AN - SCOPUS:77955413685

SN - 1567-7249

VL - 10

SP - 464

EP - 471

JO - Mitochondrion

JF - Mitochondrion

IS - 5

ER -

Phosphorylation pattern of the NDUFS4 subunit of complex I of the mammalian respiratory chain

Abstract

Keywords

ASJC Scopus subject areas

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