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1 ng domains of caveolins 1 and 3 but not with caveolin 2.
2  with increased expression of caveolin 1 and caveolin 2.
3 antly decreased expression of caveolin-1 and caveolin-2.
4  of caveolin-1 but contain normal amounts of caveolin-2.
5  cell-type and tissue-specific expression of caveolin-2.
6 caveolin gene has been identified and termed caveolin-2.
7 orming gene 1, Polo-like kinase 1 (PLK1) and Caveolin-2.
8 rom a complex of the proteins caveolin-1 and caveolin-2.
9 ly up-regulates the expression of endogenous caveolin-2.
10 n-1 expression on the behavior of endogenous caveolin-2.
11                They were cofractionated with caveolin-2, a lipid-raft-associated intracellular membra
12 colocalizes with caveolin-1, indicating that caveolin-2 also localizes to caveolae.
13 ysis of 6538 genes revealed that caveolin 1, caveolin 2, amphiregulin, and melanoma growth stimulator
14 e cell population (>95%) that also expressed caveolin 2 and GLUT4 with very low levels of the PDGF re
15 failed to interact with full-length forms of caveolin-2 and caveolin-3.
16 oid (FRT) cells, which express low levels of caveolin-2 and no caveolin-1, caveolin-2 localizes exclu
17 co-immunoprecipitation experiments show that caveolin-2 and Ras-GAP are constitutively associated in
18                                              Caveolins 2 and 3 were also detected in purified caveoli
19 latively low levels of the insulin receptor, caveolin 2, and GLUT4.
20                         Notably, caveolin-1, caveolin-2, and annexin A2, which are proteins associate
21 e commonly down-regulated genes, caveolin-1, caveolin-2, and GDF10/BMP3b, were chosen for further stu
22 marily stimulated Akt phosphorylation in the caveolin 2- and GLUT4-negative cell population.
23 stimulated the phosphorylation of Akt in the caveolin 2- and GLUT4-positive cells, whereas PDGF prima
24                                 Two of three caveolin-2 antibodies show little basal staining, but st
25 d raft-dependent tyrosine phosphorylation of caveolin-2 appeared to be a critical regulator of P. aer
26                mRNAs for both caveolin-1 and caveolin-2 are most abundantly expressed in white adipos
27           In MDCK cells, both caveolin-1 and caveolin-2 associated with low density Triton-insoluble
28 g caveolins, we show that phosphorylation of caveolin-2 at serines 23 and 36 can be differentially re
29 reatment led to the exclusion of caveolin-1, caveolin-2, beta1-adrenergic receptors (beta1-AR), beta2
30 throleukemic cell line, K562, that expresses caveolin-2 but fails to express detectable levels of cav
31 ion of lung epithelial cells is dependent on caveolin-2 but not caveolin-1.
32 noclonal antibody probe that recognizes only caveolin-2, but not caveolins-1 and -3.
33 ectly address the functional significance of caveolin-2 by genetically targeting the caveolin-2 locus
34 mains, where it decreases phosphorylation of caveolin-2 by inactivating c-Src.
35                           Phosphorylation of caveolin-2 by Src family kinases is an essential event f
36                                              Caveolin-2 (Cav-2), a member of caveolin protein family,
37 tric inhibitory polypeptide receptor (GIPR), caveolin 2 (CAV2), and peptidase D (PEPD) (P-interaction
38  composed primarily of caveolin-1 (Cav1) and caveolin-2 (Cav2) proteins.
39                                              Caveolin-2 colocalizes with caveolin-1, indicating that
40 esults in Group V PLA2 being associated with caveolin-2-containing granules close to the perinuclear
41 reduced in Cav-1-null mice, we conclude that caveolin-2 deficiency is the clear culprit in this lung
42 upregulation of serine 23 phosphorylation of caveolin-2 depends on caveolin-1-driven targeting to pla
43    In FRT cells, endogenous or overexpressed caveolin-2 did not associate with low density Triton ins
44 ar distribution, endogenous or overexpressed caveolin-2 did not promote the assembly of caveolae; rat
45 current, whereas antibodies to caveolin-1 or caveolin-2 did not.
46                      However, caveolin-1 and caveolin-2 differ in their functional interactions with
47 bodies directed against either caveolin-1 or caveolin-2 directly show that these molecules form a sta
48 l signaling genes including RhoB, PTGF-beta, caveolin-2, Egr-1, myosin 1B, and EHM2.
49                                Peptides from caveolin-2 exhibited no effect, whereas caveolin-1 and -
50         We therefore examined caveolin-1 and caveolin-2 expression in resident and thioglycollate-eli
51                                           As caveolin-2 expression is also severely reduced in Cav-1-
52 nerve growth factor (NGF) treatment, whereas caveolin-2 expression is transiently up-regulated early
53 -localization, it appears that regulation of caveolin-2 expression occurs independently of the expres
54  show a approximately 95% down-regulation in caveolin-2 expression; these cells also do not express c
55 nds, whereas the corresponding domain within caveolin-2 fails to recognize these ligands under the sa
56 udomonas co-opts the endocytic properties of caveolin-2 for invasion, there also exists in these cell
57 st, in the absence of caveolin-1 expression, caveolin-2 forms low molecular mass oligomers that are r
58 ular machinery to induce the dissociation of caveolin-2 from caveolin-1 oligomers.
59 -expression is required for the transport of caveolin-2 from the Golgi complex to the plasma membrane
60                The CAV1/CAV2 (caveolin 1 and caveolin 2) genomic region previously was associated wit
61 signed microarrays showed down-regulation of caveolin 2, GNB4, and lipase A in AD Rac1b-positive/p75(
62 t notably adipocytes and endothelial cells), caveolin-2 has traditionally been considered the dispens
63  c-Src, NCK, and Ras-GAP, that interact with caveolin-2 in a phosphorylation-dependent manner.
64          Conversely, transient expression of caveolin-2 in CHO cells is sufficient to up-regulate end
65  phenotypes, indicating a selective role for caveolin-2 in lung function.
66  show for the first time a specific role for caveolin-2 in mammalian physiology independent of caveol
67 ible involvement of serine 36-phosphorylated caveolin-2 in modulating mitosis.
68 ression of caveolin-1 or caveolin-3, but not caveolin-2, in Cav-1 null cells complements this phenoty
69 lates caveolin-1 protein expression, but not caveolin-2, in cultured NIH 3T3 and Rat 1 cells.
70 vesicles, but does not affect trafficking of caveolin-2, interaction with caveolin-1 or its biophysic
71                      At the level of the ER, caveolin-2 interacts with caveolin-1 to form a high mole
72                                              Caveolin-2 is a member of the caveolin gene family with
73                 Thus, the phosphorylation of caveolin-2 is a novel mechanism to regulate the dynamics
74     Here, we present the first evidence that caveolin-2 is a phosphoprotein.
75                          It is believed that caveolin-2 is an "accessory protein" that functions in c
76                                              Caveolin-2 is an accessory molecule and the binding part
77                                     Although caveolin-2 is coexpressed and heterooligomerizes with ca
78 ine residues and that the phosphorylation of caveolin-2 is necessary for its actions as a positive re
79                                     However, caveolin-2 is not required for caveolae formation, imply
80               More importantly, we show that caveolin-2 is phosphorylated in vivo at two serine resid
81                                              Caveolin-2 is the least well studied member of the caveo
82 ient in all three caveolin gene products, as caveolin-2 is unstable in the absence of caveolin-1.
83                               Interestingly, caveolin-2 is up-regulated in response to the mechanical
84 ation event was selective for caveolin-1, as caveolin-2 levels remained constant under these conditio
85           Ultrastructurally, this pattern of caveolin-2 localization corresponds to caveolae membrane
86 nstitutively express both caveolin-1 and -2, caveolin-2 localized to both the Golgi complex and to th
87  low levels of caveolin-2 and no caveolin-1, caveolin-2 localizes exclusively to the Golgi complex bu
88 e of caveolin-2 by genetically targeting the caveolin-2 locus (Cav-2) in mice.
89 ence of caveolin-1, serine 23-phosphorylated caveolin-2 mostly localizes to plasma membrane, while se
90                                              Caveolin-2 mRNA and protein expression were unchanged ov
91          Northern blot analysis reveals that caveolin-2 mRNA levels remain constant under these condi
92                                              Caveolin-2, on the other hand, is expressed in all cells
93 noviral transduction of either caveolin-1 or caveolin-2 or both isoforms into cells lacking both cave
94    These data support a role for caveolin 1, caveolin 2, or both in POAG and suggest that the caveoli
95               We also found that caveolin-1, caveolin-2, or Cav-1 S80E formed immunoprecipitable comp
96 of caveolin-1 in endothelial cells decreases caveolin-2 phosphorylation at serine 23 but not at serin
97 ceptor in the insulin receptor-, GLUT4-, and caveolin 2-positive cells resulted in the ability of PDG
98  lacking both caveolins, we demonstrate that caveolin-2 positively regulates caveolin-1-dependent cav
99 s revealed that serine 23 phosphorylation of caveolin-2 preferably occurs in detergent-resistant memb
100 sma membrane, while serine 36-phosphorylated caveolin-2 primarily resides in intracellular compartmen
101                              This pattern of caveolin-2 protein expression most closely resembles the
102                            In the absence of caveolin-2 protein expression, caveolae still form and c
103 embryos reveals the following: (i) a loss of caveolin-2 protein expression; (ii) defects in the endoc
104  cell and tissue types demonstrates that the caveolin-2 protein is most abundantly expressed in endot
105                                        Also, caveolin-2 protein levels remain unchanged during the di
106 o oncogenic transformation of NIH 3T3 cells, caveolin-2 protein levels remain unchanged.
107 MP2 in NIH3T3 cells decreased caveolin-1 and caveolin-2 protein levels while increasing the surface e
108 ex between caveolins-1 and -2 stabilizes the caveolin-2 protein product and allows caveolin-2 to be t
109 in-1 expression is required to stabilize the caveolin-2 protein product, to mediate the caveolar endo
110  the expression of caveolin-1 stabilizes the caveolin-2 protein.
111 1 and -3, but not the analogous regions from caveolin-2, resulted in inhibition of eNOS, inducible NO
112 rol efflux by HDL(3) leads to caveolin-1 and caveolin-2 secretion to the cell culture medium, a proce
113 tion of the primary phosphorylation sites on caveolin-2, serine 23 and 36, reduces the number of plas
114                      Decreased expression of caveolin-2 significantly impaired the ability of P. aeru
115  Cav-1-F92A was measured by stabilization of caveolin-2, sucrose gradient, and electron microscopy.
116 es the caveolin-2 protein product and allows caveolin-2 to be transported from the Golgi complex to t
117  recombinant expression of caveolin-1 allows caveolin-2 to form high molecular mass oligomers that ar
118 onclude that the tyrosine phosphorylation of caveolin-2 (Tyr(P)(19)) may function as a signal that is
119  both induce the tyrosine phosphorylation of caveolin-2 (Tyr(P)(19)).
120  differentiated PC12 cells; up-regulation of caveolin-2 under these conditions is strictly dependent
121                                 We show that caveolin-2 undergoes Src-induced phosphorylation on tyro
122                 The cellular distribution of caveolin 2 was similar to that of caveolin 1.
123                           Some overexpressed caveolin-2 was also present in lipid droplets.
124 proximately 20-kDa caveolin-related protein, caveolin-2, was identified through microsequencing of ad
125  in regulating phosphorylation of endogenous caveolin-2, we have used the siRNA approach.
126 presence of PIM1, whereas IL6, cyclin A1 and caveolin 2 were increased.
127 ace, does not co-localize significantly with caveolin-2, which is present primarily in the Golgi comp

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