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Analysis of a sub-proteome which co-purifies with and is phosphorylated by the Golgi casein kinase

Tibaldi, E; Arrigoni, G; Brunati, AM; James, Peter LU and Pinna, LA (2006) In Cellular and Molecular Life Sciences1997-01-01+01:00 63(3). p.378-389
Abstract
In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the phosphorylation of caseins in lactating mammary gland, the proteins present in fractions enriched in G-CK activity eluted from DEAE-Sepharose and heparin-Sepharose columns were resolved by two-dimensional electrophoresis and analyzed by mass spectrometry. This led to the identification of 47 proteins altogether, none of which is a bona fide protein kinase. At least 9 of the identified proteins however, are readily phosphorylated by co-purifying G-CK activity, and 7 are physically associated with it to give supramolecular complex(es) of about 500 kDa as judged from Superdex S200 gel fitration and glycerol gradient... (More)
In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the phosphorylation of caseins in lactating mammary gland, the proteins present in fractions enriched in G-CK activity eluted from DEAE-Sepharose and heparin-Sepharose columns were resolved by two-dimensional electrophoresis and analyzed by mass spectrometry. This led to the identification of 47 proteins altogether, none of which is a bona fide protein kinase. At least 9 of the identified proteins however, are readily phosphorylated by co-purifying G-CK activity, and 7 are physically associated with it to give supramolecular complex(es) of about 500 kDa as judged from Superdex S200 gel fitration and glycerol gradient ultracentrifugation experiments. In contrast, the apparent molecular weight of G-CK estimated from an in gel activity assay after SDSPAGE and renaturation is about 41 kDa. Many of the proteins phosphorylated by and/or associated with G-CK belong to the category of chaperonines, including HSP90, GRP-94 and -78, and various isoforms of protein disulfide isomerases, suggesting a global role of this kinase in the modulation of protein folding. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
chaperone, phosphoprotein, staurosporine, phosphoproteome, mammary gland, casein kinase, Golgi apparatus
in
Cellular and Molecular Life Sciences1997-01-01+01:00
volume
63
issue
3
pages
378 - 389
publisher
Birkhaüser
external identifiers
  • wos:000235139200010
  • pmid:16429323
  • scopus:32044449861
ISSN
1420-9071
DOI
10.1007/s00018-005-5506-4
language
English
LU publication?
yes
id
8f157c82-e99e-4394-8550-c43c5cc918a0 (old id 418261)
date added to LUP
2007-10-20 11:29:43
date last changed
2019-05-21 02:42:29
@article{8f157c82-e99e-4394-8550-c43c5cc918a0,
  abstract     = {In an attempt to gain information about the identity of the Golgi apparatus casein kinase(s) (G-CK), responsible for the phosphorylation of caseins in lactating mammary gland, the proteins present in fractions enriched in G-CK activity eluted from DEAE-Sepharose and heparin-Sepharose columns were resolved by two-dimensional electrophoresis and analyzed by mass spectrometry. This led to the identification of 47 proteins altogether, none of which is a bona fide protein kinase. At least 9 of the identified proteins however, are readily phosphorylated by co-purifying G-CK activity, and 7 are physically associated with it to give supramolecular complex(es) of about 500 kDa as judged from Superdex S200 gel fitration and glycerol gradient ultracentrifugation experiments. In contrast, the apparent molecular weight of G-CK estimated from an in gel activity assay after SDSPAGE and renaturation is about 41 kDa. Many of the proteins phosphorylated by and/or associated with G-CK belong to the category of chaperonines, including HSP90, GRP-94 and -78, and various isoforms of protein disulfide isomerases, suggesting a global role of this kinase in the modulation of protein folding.},
  author       = {Tibaldi, E and Arrigoni, G and Brunati, AM and James, Peter and Pinna, LA},
  issn         = {1420-9071},
  keyword      = {chaperone,phosphoprotein,staurosporine,phosphoproteome,mammary gland,casein kinase,Golgi apparatus},
  language     = {eng},
  number       = {3},
  pages        = {378--389},
  publisher    = {Birkhaüser},
  series       = {Cellular and Molecular Life Sciences1997-01-01+01:00},
  title        = {Analysis of a sub-proteome which co-purifies with and is phosphorylated by the Golgi casein kinase},
  url          = {http://dx.doi.org/10.1007/s00018-005-5506-4},
  volume       = {63},
  year         = {2006},
}