Filling in the Gap in Galectin-1 Export
Abstract
Many of the eukaryotic secreted proteins generally contain a leader- or export sequence, which directs their synthesis to the endoplasmic reticulum (ER). The secreted proteins are cotranslationally inserted into the ER lumen and are then trafficked to the Golgi and transport vesicles, which fuse with the plasma membrane to release their content to the extracellular space. Interestingly, galectins, fibroblast growth factor (FGF) 1 and 2 (1), interleukin (IL) 1b (2), the human immunodeficiency virus-1 (HIV-1) transactivating protein TAT (3) and the Herpes virus structural protein VP22 (4) are examples of proteins that do not contain leader sequence. While the mechanism of secretion of proteins lacking signal sequence is unknown, IL-1b, FGF-1 and FGF-2 appears to utilize shedding of membrane as vesicles as modules in their secretion (5). HIV-1 TAT, however, seems to be transported directly across the plasma membrane. However, the mechanism by which galectin-1 is secreted is unknown, which is described non-conventional.
Document Details
- Document Type
- Technical Report
- Publication Date
- Sep 01, 2007
- Accession Number
- ADA475020
Entities
People
- Subrahmanyeswara U. Rao
Organizations
- Texas Tech University Health Sciences Center