2010
DOI: 10.1074/jbc.m110.106278
|View full text |Cite
|
Sign up to set email alerts
|

PKA Regulates Vacuolar H+-ATPase Localization and Activity via Direct Phosphorylation of the A Subunit in Kidney Cells

Abstract: Acid secretion in epithelial cells is actively regulated by environmental signals, although the mechanisms by which these cues are translated into activation of H ϩ transport pathways remains the subject of intense research (11,(15)(16)(17)(18)(19). For example, the V-ATPase is regulated by several pathways, which involve CO 2 , phosphatidylinositol 3-kinase, aldolase, phosphofructokinase, actin, microtubules, and angiotensin in a variety of mammalian cellular systems (20 -27). The number of VATPases at the ap… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

3
111
0
1

Year Published

2012
2012
2023
2023

Publication Types

Select...
6
1
1

Relationship

2
6

Authors

Journals

citations
Cited by 95 publications
(116 citation statements)
references
References 64 publications
3
111
0
1
Order By: Relevance
“…These findings have led to an intense search for the pHsensing mechanism within the intercalated cells. For example, the H 1 -ATPase in type A intercalated cells is acutely activated (within minutes to hours) by kinases such as protein kinase A (PKA), while it is acutely inhibited by the metabolic sensor AMP activated protein kinase (AMPK) ( Figure 5) (72)(73)(74). This downregulation of the proton pump by AMPK is preliminary evidence that intercalated cell function can be altered when the tubule is under metabolic stress, such as under conditions of ischemia.…”
Section: Acid-base Sensing In Intercalated Cellsmentioning
confidence: 93%
“…These findings have led to an intense search for the pHsensing mechanism within the intercalated cells. For example, the H 1 -ATPase in type A intercalated cells is acutely activated (within minutes to hours) by kinases such as protein kinase A (PKA), while it is acutely inhibited by the metabolic sensor AMP activated protein kinase (AMPK) ( Figure 5) (72)(73)(74). This downregulation of the proton pump by AMPK is preliminary evidence that intercalated cell function can be altered when the tubule is under metabolic stress, such as under conditions of ischemia.…”
Section: Acid-base Sensing In Intercalated Cellsmentioning
confidence: 93%
“…For example, enhanced “delivery” from V‐ATPase‐rich intracellular vesicles increases the density of the complex in the apical plasma membrane of renal intercalated cells in response to reduced plasma pH 12. Here, PKA‐mediated phosphorylation of V‐ATPase controls fusion and endocytosis of V‐ATPase‐containing vesicles 13, 14. Interestingly, the PKA‐mediated increase in apical V‐ATPase in epididymal clear cells and renal intercalated cells is antagonized by AMPK and the V 1 A subunit appears to be a shared target for modulation by PKA and AMPK‐mediated phosphorylation 14, 15.…”
Section: V‐atpase Structure and Function In Normal Physiologymentioning
confidence: 99%
“…Here, PKA‐mediated phosphorylation of V‐ATPase controls fusion and endocytosis of V‐ATPase‐containing vesicles 13, 14. Interestingly, the PKA‐mediated increase in apical V‐ATPase in epididymal clear cells and renal intercalated cells is antagonized by AMPK and the V 1 A subunit appears to be a shared target for modulation by PKA and AMPK‐mediated phosphorylation 14, 15. Additionally, the V o a subunits are important for targeting V‐ATPases to the plasma membrane of specialized acidifying cells.…”
Section: V‐atpase Structure and Function In Normal Physiologymentioning
confidence: 99%
“…The V-ATPase is a well-known downstream target of protein kinases in a variety of systems (Voss et al, 2007;Hallows et al, 2009;Alzamora et al, 2010), and the involvement of cAMP in diuresis suggests that this is also the case in Malpighian tubules of A. aegypti (Williams and Beyenbach, 1983;Sawyer and Beyenbach, 1985).…”
Section: V-atpase Activation Can Occur Via Pka-dependent and Pkaindepmentioning
confidence: 99%