ER exit sites (ERES) and ER–mitochondria encounter structures (ERMES) often localize proximally. Issue 2 (21st October 2022)

• Record Type: Journal Article
• Authors: Chakraborty, Naini; Jain, Bhawik Kumar; Shembekar, Samruddhi; Bhattacharyya, Dibyendu
• Is Part Of: FEBS letters. Volume 597:Issue 2(2023)
• Page Start: 320
• Page End: 336
• Publication Date: 2022-10-21
• Subjects: ER -- ERES -- ERMES -- Golgi -- mitochondria; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.14497
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : To understand the potential interplay between vesicular trafficking and direct membrane contact sites‐mediated transport, we selected the endoplasmic reticulum (ER), which participates in both modes of inter‐organelle transport. ER–mitochondria encounter structures (ERMES) are direct membrane contact junctions that mediate macromolecule exchange, while the secretory pathway originates at ER exit sites (ERES). Using the budding yeast Pichia pastoris, we documented that ERMES resident proteins are often juxtaposed with ERES markers. We further demonstrated that ERES form de novo almost always near a pre‐existing ERMES. Disruption of either ERES or ERMES affects the other. Djp1, a chaperone reported to mediate mitochondrial import of ER‐resident proteins, localizes at the ERES–ERMES proximal region. Our results indicate a potential functional link between ERES–ERMES proximity and mitochondrial protein import. Abstract : We demonstrated that endoplasmic reticulum (ER) exit sites (ERES) and ER–mitochondria encounter structures (ERMES) are often found in a juxtaposed position in the budding yeast Pichia pastoris . The observation indicates a potential link between vesicular trafficking and transport mediated by direct membrane contact sites. Our data also suggest that such proximal location of ERES and ERMES is potentially important for certain types of mitochondrial import.