Molecular Determinants of tGolgin-1 Function
Abstract
TGolgin-1 is a large peripheral membrane protein that consitsts predominantly of coiled coil regions and associates with the trans Golgi network (TGN) by virtue of a C-terminal GRIP domain. Our work has shown that overexpression of isolated GRIP domains from tGolgin-1 or a related protein, golgin-97, results in disruption of the structure, protein content, and function of the TGN, suggesting that tGolgin-1 and other GRIP domain proteins function in regulating TGN structure and function. This is important because signalling molecules required for initiating transformation and for metastasis rely on sorting and processing in the TGN. We have established tools to dissect the molecular basis of GRIP domain function and of the predicted N- terminal domain. More recently we have successfully used RNAi to eliminate expression of tGolgin-1 from mammalian cells. The results suggest that tGolgin-1 may play a more broad role in positioning the Golgi complex at the microtubule organizing center of the cell. This has important implications for a role of tGolgin-1 in cell motility required both for tumor metastasis and for the targeting of tumors by inflammatory cells and cytotoxic T lymphocytes.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2002
- Accession Number
- ADA408101
Entities
People
- Atsuko Yoshino
- Mark A. Lemmon
- Michael S. Marks
Organizations
- University of Pennsylvania