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Molecular Diversity of Plasma Membrane Ca2+ Transporting ATPases: Their Function Under Normal and Pathological Conditions

  • Luca Hegedűs
  • Boglárka Zámbó
  • Katalin Pászty
  • Rita Padányi
  • Karolina Varga
  • John T. Penniston
  • Ágnes EnyediEmail author
Chapter
First Online:
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1131)

Abstract

Plasma membrane Ca2+ transport ATPases (PMCA1-4, ATP2B1-4) are responsible for removing excess Ca2+ from the cell in order to keep the cytosolic Ca2+ ion concentration at the low level essential for normal cell function. While these pumps take care of cellular Ca2+ homeostasis they also change the duration and amplitude of the Ca2+ signal and can create Ca2+ gradients across the cell. This is accomplished by generating more than twenty PMCA variants each having the character – fast or slow response, long or short memory, distinct interaction partners and localization signals – that meets the specific needs of the particular cell-type in which they are expressed. It has become apparent that these pumps are essential to normal tissue development and their malfunctioning can be linked to different pathological conditions such as certain types of neurodegenerative and heart diseases, hearing loss and cancer. In this chapter we summarize the complexity of PMCA regulation and function under normal and pathological conditions with particular attention to recent developments of the field.

Keywords

Plasma membrane Ca2+ ATPase (PMCA) ATP2B1-4 Alternative splice Calmodulin Phosphatidylinositol-45-bisphosphate Actin cytoskeleton Ca2+ signal Genetic variation Altered expression Pathological condition 

Abbreviations

AD

Alzheimer’s disease

ATP

adenosine triphosphate

CaM

calmodulin

CaMKII

calcium/calmodulin-dependent protein kinase II

CASK

calcium/calmodulin-dependent serine protein kinase

CBS

calmodulin binding sequence

ER

endoplasmic reticulum

ERK

extracellular-signal regulated kinase

HDAC

histone deacetylase

HER2

human epidermal growth factor receptor 2

HUVEC

human umbilical vein endothelial cell

IP3

inositol 1,4,5-trisphosphate

IP3R

inositol 1,4,5-trisphosphate receptor

IS

immunological synapse

MAGUK

membrane-associated guanylate kinase

MLEC

mouse lung endothelial cells

NFAT

nuclear factor of activated T-cell

NHERF2

Na+/H+ exchanger regulatory factor 2

nNOS

neural nitric oxide synthase

PIP2

phosphatidylinositol-4,5- bisphosphate

PKC

protein kinase C

PKA

protein kinase A

PMCA

plasma membrane Ca2+ ATPases

POST

partner of STIM

PSD-95

post synaptic density protein 95

RANKL

nuclear factor κB ligand

RASSF1

Ras association domain-containing protein 1

RBC

red blood cell

SCD

sickle cell disease

SERCA

sarco/endoplasmic reticulum Ca2+ ATPases

SNP

small nucleotide polymorphisms

SOCE

store operated Ca2+ entry

SPCA

secretory-pathway Ca2+ ATPase

STIM

stromal interacting molecule

TGF

transforming growth factor

TM domain

transmembrane domain

TSA

trichostatin A

VEGF

vascular endothelial growth factor

VSMC

vascular smooth muscle cell

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Notes

Acknowledgement

The authors are supported by grants from the Hungarian Scientific Research Funds NKFIH K119223 and FIKP-EMMI (AE).

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© Springer Nature Switzerland AG 2020

Authors and Affiliations

  • Luca Hegedűs
    • 1
  • Boglárka Zámbó
    • 2
  • Katalin Pászty
    • 3
  • Rita Padányi
    • 4
  • Karolina Varga
    • 4
  • John T. Penniston
    • 5
  • Ágnes Enyedi
    • 4
    Email author
  1. 1.Department of Thoracic Surgery, RuhrlandklinikUniversity Clinic EssenEssenGermany
  2. 2.Research Centre for Natural SciencesInstitute of Enzymology, Hungarian Academy of SciencesBudapestHungary
  3. 3.Department of BiophysicsSemmelweis UniversityBudapestHungary
  4. 4.2nd Department of PathologySemmelweis UniversityBudapestHungary
  5. 5.Department of NeurosurgeryMassachusetts General HospitalBostonUSA

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