IDENTIFICATION OF PLAKOGLOBIN DOMAINS REQUIRED FOR ASSOCIATION WITH N-CADHERIN AND ALPHA-CATENIN

被引:131
作者
SACCO, PA [1 ]
MCGRANAHAN, TM [1 ]
WHEELOCK, MJ [1 ]
JOHNSON, KR [1 ]
机构
[1] UNIV TOLEDO,DEPT BIOL,TOLEDO,OH 43606
关键词
D O I
10.1074/jbc.270.34.20201
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified, The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule, In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show that the alpha-catenin-binding region maps within the first repeat and the N-cadherin binding region maps within repeats 7 and 8.
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页码:20201 / 20206
页数:6
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