Visualizing CaMKII and CaM activity

A paradigm of compartmentalized signaling

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Calcium (Ca2+) has long been recognized as a crucial intracellular messenger attaining stimuli-specific cellular outcomes via localized signaling. Ca2+-binding proteins, such as calmodulin (CaM), and its target proteins are key to the segregation and refinement of these Ca2+-dependent signaling events. This review not only summarizes the recent technological advances enabling the study of subcellular Ca 2+-CaM and Ca2+-CaM-dependent protein kinase (CaMKII) signaling events but also highlights the outstanding challenges in the field.

Original languageEnglish (US)
Pages (from-to)907-916
Number of pages10
JournalJournal of Molecular Medicine
Volume91
Issue number8
DOIs
StatePublished - Aug 2013

Fingerprint

Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calmodulin
Calcium-Calmodulin-Dependent Protein Kinases
Carrier Proteins
Calcium
Proteins

Keywords

  • Ca-calmodulin-dependent protein kinase II (CaMKII)
  • Calcium
  • Calmodulin

ASJC Scopus subject areas

  • Molecular Medicine
  • Drug Discovery
  • Genetics(clinical)

Cite this

Visualizing CaMKII and CaM activity : A paradigm of compartmentalized signaling. / Bossuyt, Julie B C; Bers, Donald M.

In: Journal of Molecular Medicine, Vol. 91, No. 8, 08.2013, p. 907-916.

Research output: Contribution to journalArticle

@article{b43ca875ad154293973b1ca14335332f,
title = "Visualizing CaMKII and CaM activity: A paradigm of compartmentalized signaling",
abstract = "Calcium (Ca2+) has long been recognized as a crucial intracellular messenger attaining stimuli-specific cellular outcomes via localized signaling. Ca2+-binding proteins, such as calmodulin (CaM), and its target proteins are key to the segregation and refinement of these Ca2+-dependent signaling events. This review not only summarizes the recent technological advances enabling the study of subcellular Ca 2+-CaM and Ca2+-CaM-dependent protein kinase (CaMKII) signaling events but also highlights the outstanding challenges in the field.",
keywords = "Ca-calmodulin-dependent protein kinase II (CaMKII), Calcium, Calmodulin",
author = "Bossuyt, {Julie B C} and Bers, {Donald M}",
year = "2013",
month = "8",
doi = "10.1007/s00109-013-1060-y",
language = "English (US)",
volume = "91",
pages = "907--916",
journal = "Journal of Molecular Medicine",
issn = "0946-2716",
publisher = "Springer Verlag",
number = "8",

}

TY - JOUR

T1 - Visualizing CaMKII and CaM activity

T2 - A paradigm of compartmentalized signaling

AU - Bossuyt, Julie B C

AU - Bers, Donald M

PY - 2013/8

Y1 - 2013/8

N2 - Calcium (Ca2+) has long been recognized as a crucial intracellular messenger attaining stimuli-specific cellular outcomes via localized signaling. Ca2+-binding proteins, such as calmodulin (CaM), and its target proteins are key to the segregation and refinement of these Ca2+-dependent signaling events. This review not only summarizes the recent technological advances enabling the study of subcellular Ca 2+-CaM and Ca2+-CaM-dependent protein kinase (CaMKII) signaling events but also highlights the outstanding challenges in the field.

AB - Calcium (Ca2+) has long been recognized as a crucial intracellular messenger attaining stimuli-specific cellular outcomes via localized signaling. Ca2+-binding proteins, such as calmodulin (CaM), and its target proteins are key to the segregation and refinement of these Ca2+-dependent signaling events. This review not only summarizes the recent technological advances enabling the study of subcellular Ca 2+-CaM and Ca2+-CaM-dependent protein kinase (CaMKII) signaling events but also highlights the outstanding challenges in the field.

KW - Ca-calmodulin-dependent protein kinase II (CaMKII)

KW - Calcium

KW - Calmodulin

UR - http://www.scopus.com/inward/record.url?scp=84881254621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84881254621&partnerID=8YFLogxK

U2 - 10.1007/s00109-013-1060-y

DO - 10.1007/s00109-013-1060-y

M3 - Article

VL - 91

SP - 907

EP - 916

JO - Journal of Molecular Medicine

JF - Journal of Molecular Medicine

SN - 0946-2716

IS - 8

ER -