PMID- 10556585
OWN - NLM
STAT- MEDLINE
DCOM- 19991124
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1451
IP  - 2-3
DP  - 1999 Sep 21
TI  - Modulation of Xenopus oocyte-expressed phospholemman-induced ion currents by
      co-expression of protein kinases.
PG  - 305-18
AB  - Phospholemman (PLM), the major sarcolemmal substrate for phosphorylation by
      cAMP-dependent kinase (PKA) protein kinase C (PKC) and NIMA kinase in muscle,
      induces hyperpolarization-activated anion currents in Xenopus oocytes, most
      probably by enhancing endogenous oocyte currents. PLM peptides from the
      cytoplasmic tail are phosphorylated by PKA at S68, by NIMA kinase at S63, and by 
      PKC at both S63 and S68. We have confirmed the phosphorylation sites in the
      intact protein, and we have investigated the role of phosphorylation in the
      regulatory activity of PLM using oocyte expression experiments. We found: (1) the
      cytoplasmic domain is not essential for inducing currents in oocytes; (2)
      co-expression of PKA increased the amplitude of oocyte currents and the amount of
      PLM in the oocyte membrane largely, but not exclusively, through phosphorylation 
      of S68; (3) co-expression of PKA had no effect on a PLM mutant in which all
      putative phosphorylation sites had been inactivated by serine to alanine mutation
      (SSST 62, 63, 68, 69 AAAA); (4) co-expression of PKC had no effect in this
      system; (5) co-expression of NIMA kinase increased current amplitude and membrane
      protein level, but did not require PLM phosphorylation. These findings point to a
      role for phosphorylation in the function of PLM.
FAU - Mounsey, J P
AU  - Mounsey JP
AD  - Department of Internal Medicine (Cardiovascular Division), University of Virginia
      Health Sciences Center, Charlottesville, VA 22908, USA. pmounsey@virginia.edu
FAU - Lu, K P
AU  - Lu KP
FAU - Patel, M K
AU  - Patel MK
FAU - Chen, Z H
AU  - Chen ZH
FAU - Horne, L T
AU  - Horne LT
FAU - John, J E 3rd
AU  - John JE 3rd
FAU - Means, A R
AU  - Means AR
FAU - Jones, L R
AU  - Jones LR
FAU - Moorman, J R
AU  - Moorman JR
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Chloride Channels)
RN  - 0 (Ion Channels)
RN  - 0 (Membrane Proteins)
RN  - 0 (Phosphoproteins)
RN  - 135541-82-1 (phospholemman)
RN  - EC 2.7.- (Protein Kinases)
RN  - EC 2.7.11.1 (NIMA-Related Kinase 1)
RN  - EC 2.7.11.1 (NIMA-Related Kinases)
RN  - EC 2.7.11.1 (NIMA-related kinase 6)
RN  - EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
RN  - EC 2.7.11.13 (Protein Kinase C)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Binding Sites
MH  - *Cell Cycle Proteins
MH  - Cell Membrane/metabolism
MH  - Chloride Channels/biosynthesis
MH  - Cyclic AMP-Dependent Protein Kinases/biosynthesis
MH  - Gene Expression
MH  - Ion Channels/*biosynthesis
MH  - Membrane Proteins/chemistry/*metabolism
MH  - Molecular Sequence Data
MH  - NIMA-Related Kinase 1
MH  - NIMA-Related Kinases
MH  - Oocytes/*metabolism
MH  - Phosphoproteins/chemistry/*metabolism
MH  - Phosphorylation
MH  - Protein Kinase C/biosynthesis
MH  - Protein Kinases/*biosynthesis
MH  - Protein-Serine-Threonine Kinases/biosynthesis
MH  - Up-Regulation
MH  - Xenopus
EDAT- 1999/11/11 09:00
MHDA- 2001/03/28 10:01
CRDT- 1999/11/11 09:00
PHST- 1999/11/11 09:00 [pubmed]
PHST- 2001/03/28 10:01 [medline]
PHST- 1999/11/11 09:00 [entrez]
AID - S0167-4889(99)00102-0 [pii]
AID - 10.1016/s0167-4889(99)00102-0 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1999 Sep 21;1451(2-3):305-18. doi:
      10.1016/s0167-4889(99)00102-0.