NDLI: Structural characterization of the membrane-associated regulatory subunit of type I cAMP-dependent protein kinase by mass spectrometry: identification of Ser81 as the in vivo phosphorylation site of RIalpha.

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Structural characterization of the membrane-associated regulatory subunit of type I cAMP-dependent protein kinase by mass spectrometry: identification of Ser81 as the in vivo phosphorylation site of RIalpha.

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Structural characterization of the membrane-associated regulatory subunit of type I cAMP-dependent protein kinase by mass spectrometry: identification of Ser81 as the in vivo phosphorylation site of RIalpha.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Boeshans, K. M. Shabb, J. B. Hunt, J. B. Resing, K. A. Ahn, N. G.
Description	Country affiliation: United States Author Affiliation: Boeshans KM ( Department of Biochemistry and Molecular Biology, University of North Dakota, Grand Forks 58202-9037, USA.)
Abstract	The mechanism by which the type Ialpha regulatory subunit (RIalpha) of cAMP-dependent protein kinase is localized to cell membranes is unknown. To determine if structural modification of RIalpha is important for membrane association, both beef skeletal muscle cytosolic RI and beef heart membrane-associated RI were characterized by electrospray ionization mass spectrometry. Total sequence coverage was 98% for both the membrane-associated and cytosolic forms of RI after digestion with AspN protease or trypsin. Sequence data indicated that membrane-associated and cytosolic forms of RI were the same RIalpha gene product. A single RIalpha phosphorylation site was identified at Ser81 located near the autoinhibitory domain of both membrane-associated and cytosolic RIalpha. Because both R subunit preparations were 30-40% phosphorylated, this post-translational modification could not be responsible for the membrane compartmentation of the majority of RIalpha. Mass spectrometry also indicated that membrane-associated RIalpha had a higher extent of disulfide bond formation in the amino-terminal dimerization domain. No other structural differences between cytosolic and membrane-associated RIalpha were detected. Consistent with these data, masses of the intact proteins were identical by LCQ mass spectrometry. Lack of detectable structural differences between membrane-associated and cytosolic RIalpha strongly suggests an interaction between RIalpha and anchoring proteins or membrane lipids as more likely mechanisms for explaining RIalpha membrane association in the heart.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	7
Volume Number	8
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1999-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cyclic Amp-dependent Protein Kinases Chemistry Serine Amino Acid Sequence Animals Cyclic Amp-dependent Protein Kinase Rialpha Subunit Cysteine Mass Spectrometry Membrane Proteins Molecular Sequence Data Phosphorylation Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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