3.9 Article

E-Cadherin/Catenin Complexes Are Formed Cotranslationally in the Endoplasmic Reticulum/Golgi Compartments

期刊

CELL COMMUNICATION AND ADHESION
卷 15, 期 4, 页码 365-378

出版社

TAYLOR & FRANCIS INC
DOI: 10.1080/15419060802460748

关键词

E-cadherin; prosequence; catenin; N-cadherin; Golgi complex; adhesion

资金

  1. NIH [R01-DE12308, R01-GM51188]
  2. NCI [P30 CA36727]
  3. NATIONAL CANCER INSTITUTE [P30CA036727] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [R01DE012308] Funding Source: NIH RePORTER
  5. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM051188] Funding Source: NIH RePORTER

向作者/读者索取更多资源

Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.

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