PMID- 10648825
OWN - NLM
STAT- MEDLINE
DCOM- 20000222
LR  - 20190621
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 466
IP  - 1
DP  - 2000 Jan 21
TI  - Phosphorylation of the skeletal muscle glycogen-targetting subunit of protein
      phosphatase 1 in response to adrenaline in vivo.
PG  - 121-4
AB  - The protein G(M), which targets protein phosphatase 1 (PP1) to the glycogen
      particles and sarcoplasmic reticulum (SR) of striated muscles, is known to be
      phosphorylated at Ser48 and Ser67 in vitro by adenosine 3',5' cyclic
      monophosphate-dependent protein kinase (PKA) and at Ser48 by MAP kinase-activated
      protein kinase-1 (MAPKAP-K1, also called p90 RSK). The phosphorylation of Ser48
      increases the rate at which the glycogen-associated PP1.G(M) complex
      dephosphorylates (activates) glycogen synthase, but the phosphorylation of Ser67 
      has the opposite effect, suppressing the activity of PP1 toward glycogen-bound
      substrates. The phosphorylation of Ser67 overrides the activating effect of Ser48
      phosphorylation because it dissociates PP1 from G(M). Here, we use two
      phospho-specific antibodies to demonstrate that the SR-associated form of G(M),
      as well as the glycogen-associated form of G(M), becomes phosphorylated at Ser48 
      and Ser67 in response to adrenaline, supporting the view that the PKA-mediated
      regulation of the PP1.G(M) complex plays a role in the adrenergic control of
      glycogen metabolism and SR function. In contrast, Ser48 is not phosphorylated
      significantly in response to insulin, and neither is Ser67. Thus the
      phosphorylation of G(M) at Ser48 by MAPKAP-K1 or other insulin-stimulated protein
      kinases is not involved in the activation of glycogen synthase by insulin.
FAU - Walker, K S
AU  - Walker KS
AD  - MRC Protein Phosphorylation Unit, MSI/WTB Complex, University of Dundee, Dow
      Street, Dundee, UK.
FAU - Watt, P W
AU  - Watt PW
FAU - Cohen, P
AU  - Cohen P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Insulin)
RN  - 452VLY9402 (Serine)
RN  - 9005-79-2 (Glycogen)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
RN  - EC 3.1.3.16 (Protein Phosphatase 1)
RN  - YKH834O4BH (Epinephrine)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - Epinephrine/*pharmacology
MH  - Glycogen/*metabolism
MH  - Humans
MH  - In Vitro Techniques
MH  - Insulin/pharmacology
MH  - Male
MH  - Muscle, Skeletal/*drug effects/*enzymology
MH  - Phosphoprotein Phosphatases/chemistry/genetics/*metabolism
MH  - Phosphorylation
MH  - Protein Phosphatase 1
MH  - Protein Structure, Quaternary
MH  - Rabbits
MH  - Rats
MH  - Rats, Wistar
MH  - Sarcoplasmic Reticulum/enzymology
MH  - Serine/chemistry
EDAT- 2000/01/29 09:00
MHDA- 2000/02/26 09:00
CRDT- 2000/01/29 09:00
PHST- 2000/01/29 09:00 [pubmed]
PHST- 2000/02/26 09:00 [medline]
PHST- 2000/01/29 09:00 [entrez]
AID - S0014-5793(99)01771-8 [pii]
AID - 10.1016/s0014-5793(99)01771-8 [doi]
PST - ppublish
SO  - FEBS Lett. 2000 Jan 21;466(1):121-4. doi: 10.1016/s0014-5793(99)01771-8.