+ |
PKA | up-regulates activity
phosphorylation
|
PDE4A |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275985 |
Ser145 |
ATSQRREsFLYRSDS |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
12023945 |
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273937 |
Ser89 |
TRMSWPSsFHGTGTG |
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
12023945 |
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5. |
|
Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
+ |
MAPKAPK2 | down-regulates activity
phosphorylation
|
PDE4A |
0.355 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-263078 |
Ser152 |
SFLYRSDsDYDMSPK |
Homo sapiens |
Macrophage |
pmid |
sentence |
21323643 |
Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) by MK2 (MAPKAPK2) attenuates its activation through protein kinase A phosphorylation. In the present study, we show that PDE4A5 is phosphorylated at Ser147, within the regulatory UCR1 (ultraconserved region 1) domain conserved among PDE4 long isoforms, by MK2 (MAPK-activated protein kinase 2, also called MAPKAPK2). Phosphorylation by MK2, although not altering PDE4A5 activity, markedly attenuates PDE4A5 activation through phosphorylation by protein kinase A. This modification confers the amplification of intracellular cAMP accumulation in response to adenylate cyclase activation by attenuating a major desensitization system to cAMP. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |