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2014 ; 28
(9
): 3823-31
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Regulation of intracellular signaling and function by caveolin
#MMPMID24858278
Fridolfsson HN
; Roth DM
; Insel PA
; Patel HH
FASEB J
2014[Sep]; 28
(9
): 3823-31
PMID24858278
show ga
Caveolae, flask-like invaginations of the plasma membrane, were discovered nearly
60 years ago. Originally regarded as fixation artifacts of electron microscopy,
the functional role for these structures has taken decades to unravel. The
discovery of the caveolin protein in 1992 (by the late Richard G.W. Anderson)
accelerated progress in defining the contribution of caveolae to cellular
physiology and pathophysiology. The three isoforms of caveolin (caveolin-1, -2,
and -3) are caveolae-resident structural and scaffolding proteins that are
critical for the formation of caveolae and their localization of signaling
entities. A PubMed search for "caveolae" reveals ?280 publications from their
discovery in the 1950s to the early 1990s, whereas a search for "caveolae or
caveolin" after 1990, identifies ?7000 entries. Most work on the regulation of
biological responses by caveolae and caveolin since 1990 has focused on caveolae
as plasma membrane microdomains and the function of caveolin proteins at the
plasma membrane. By contrast, our recent work and that of others has explored the
localization of caveolins in multiple cellular membrane compartments and in the
regulation of intracellular signaling. Cellular organelles that contain caveolin
include mitochondria, nuclei and the endoplasmic reticulum. Such intracellular
localization allows for a complexity of responses to extracellular stimuli by
caveolin and the possibility of novel organelle-targeted therapeutics. This
review focuses on the impact of intracellular localization of caveolin on signal
transduction and cell regulation.