FEBS Lett 2006,
PMID: 16530191
Selvakumar, Ponniah; Smith-Windsor, Erin; Bonham, Keith; Sharma, Rajendra K
A number of viral and eukaryotic proteins which undergo a lipophilic modification by the enzyme N-myristoyltransferase (NMT: NMT1 and NMT2) are required for signal transduction and regulatory functions. To investigate whether NMT2 contributes to the pathogenesis of colorectal carcinoma, we observed a higher expression of NMT2 in most of the cases of cancerous tissues compared to normal tissues (84.6% of cases; P < 0.05) by Western blot analysis. Furthermore, protein-protein interaction of NMTs revealed that m-calpain interacts with NMT1 while caspase-3 interacts with NMT2. Our findings provide the first evidence of higher expression of NMT2 in human colorectal adenocarcinomas and the interaction of both forms of NMT with various signaling molecules.
Diseases/Pathways annotated by Medline MESH: Colonic Neoplasms
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Text Mining Data
Dashed line = No text mining data
Manually curated Databases
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IRef Hprd Interaction:
NMT2
—
BCL2
(in vivo)
-
IRef Hprd Interaction:
TP53
—
NMT2
(in vivo)
-
IRef Hprd Interaction:
NMT2
—
CASP3
(in vivo)
-
IRef Hprd Interaction:
TP53
—
NMT1
(in vivo)
-
IRef Hprd Interaction:
CAPN2
—
NMT1
(in vivo)
-
IRef Intact Interaction:
NMT2
—
BCL2
(physical association, anti bait coimmunoprecipitation)
-
IRef Intact Interaction:
NMT2
—
TP53
(physical association, anti bait coimmunoprecipitation)
-
IRef Intact Interaction:
NMT2
—
CASP3
(physical association, anti bait coimmunoprecipitation)
-
IRef Intact Interaction:
NMT1
—
TP53
(physical association, anti bait coimmunoprecipitation)
-
IRef Intact Interaction:
NMT1
—
CAPN2
(physical association, anti bait coimmunoprecipitation)
In total, 5 gene pairs are associated to this article in curated databases