Title :
Stromal interaction molecule 1 (
STIM1 ), a transmembrane
protein with growth suppressor activity, contains an extracellular SAM
domain modified by N-linked glycosylation
Abstract :
- Stromal interaction molecule 1 ( STIM1 ) is a cell surface transmembrane glycoprotein implicated in tumour growth control and stromal-haematopoietic cell interactions
- A single sterile alpha motif ( SAM ) protein- protein interaction domain is modelled within its extracellular region , a subcellular localisation not previously described for other SAM domain-containing proteins
- We have defined the transmembrane topology of STIM1 by determining the sites of N-linked glycosylation
- We have confirmed that STIM1 is modified by N-linked glycosylation at two sites within the SAM domain itself, deduced as asparagine residues N131 and N171 , demonstrating that STIM1 is translocated across the membrane of the endoplasmic reticulum such that the SAM domain resides within the endoplasmic reticulum (ER) lumen
- Both N-linked oligosaccharides remain endoglycosidase H-sensitive, indicating absence of full processing within the ER and Golgi
- This immature modification is nevertheless sufficient and critical for cell surface expression of STIM1
- We show that STIM1- STIM1 homotypic interactions are mediated via the cytoplasmic rather than the extracellular region of STIM1 , excluding an essential role for the SAM domain in these protein interactions
- These studies provide the first evidence for an extracellular localisation of a SAM domain within any protein , and the first example of a SAM domain modified by N-linked glycosylation
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycoprotein, , Stromal interaction molecule 1, -, -
- 1. glycoprotein, , glycoprotein, -, -
- 3. glycosylation, , -, -, sites
- 4. glycosylation, , -, -, sites
- 4. residues, , -, -, asparagine residues N131 and N171
Output(Part-Of) (sent_index,
protein,
site):
- 0. STIM1, domain
- 0. Stromal interaction molecule 1, domain
- 0. protein, domain
- 2. SAM, domain
- 2. protein, domain
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 4. Stromal interaction molecule 1, -, asparagine residues N131 and N171