GRAMD2 Blocking Peptide
- Known as:
- GRAMD2 Blocking Peptide
- Catalog number:
- 33r-5276
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- GRAMD2 Blocking Peptide
Ask about this productRelated genes to: GRAMD2 Blocking Peptide
- Gene:
- GRAMD2A NIH gene
- Name:
- GRAM domain containing 2A
- Previous symbol:
- GRAMD2
- Synonyms:
- -
- Chromosome:
- 15q23
- Locus Type:
- gene with protein product
- Date approved:
- 2005-11-02
- Date modifiied:
- 2019-02-21
Related products to: GRAMD2 Blocking Peptide
Related articles to: GRAMD2 Blocking Peptide
- GRAM domain proteins were reported as novel ER-PM tethers defining specific membrane contact sites (MCS) subdomains. GRAMD2a pre-marks the sites occupied by STIM1 at MCS and its ablation impairs STIM1 translocation, but not store-operated Ca entry. We discuss these apparently counterintuitive findings in the context of STIM/ORAI signaling at MCS. - Source: PubMed
Publication date: 2018/04/18
Nunes PaulaDemaurex Nicolas - Endoplasmic reticulum (ER) membrane contact sites (MCSs) are crucial regulatory hubs in cells, playing roles in signaling, organelle dynamics, and ion and lipid homeostasis. Previous work demonstrated that the highly conserved yeast Ltc/Lam sterol transporters localize and function at ER MCSs. Our analysis of the human family members, GRAMD1a and GRAMD2a, demonstrates that they are ER-PM MCS proteins, which mark separate regions of the plasma membrane (PM) and perform distinct functions in vivo. GRAMD2a, but not GRAMD1a, co-localizes with the E-Syt2/3 tethers at ER-PM contacts in a PIP lipid-dependent manner and pre-marks the subset of PI(4,5)P2-enriched ER-PM MCSs utilized for STIM1 recruitment. Data from an analysis of cells lacking GRAMD2a suggest that it is an organizer of ER-PM MCSs with pleiotropic functions including calcium homeostasis. Thus, our data demonstrate the existence of multiple ER-PM domains in human cells that are functionally specialized by GRAM-domain containing proteins. - Source: PubMed
Publication date: 2018/02/22
Besprozvannaya MarinaDickson EamonnLi HaoGinburg Kenneth SBers Donald MAuwerx JohanNunnari Jodi