2024 NBS Bergen Spring Symposium 10/4-24 at BBB

2024 NBS Bergen Spring Symposium 10/4-24 at BBB


If you have any feedback for the organizing committee you can register it below.


Sign up here to participate at the 2024 NBS Bergen Spring Symposium arranged by NBS Bergen with support from the Bergen Biomedical Research School (BBRS).

The symposium will be held at the third floor of Bygg for Biologiske Basalfag (BBB), Jonas Lies vei 91

08.30 – 08.45 Coffee and mingling
08.45 - 09.00 Welcoming remarks (Auditorium 4, BBB)
09.00 – 10.45 Short talks from young researchers at UiB (Audtorium 4, BBB)
10.45 – 12.00 Poster session (Vrimlearealet, BBB)
12.15 – 13.15 Key-note lecture from Jennifer Lippincott-Schwartz (Auditorium 1, BBB)

Info about the event:

There are two open spots for minisymposium lectures (12 + 3 mins). Sign up by March 17th to be considered for an oral presentation (Registration for short talks are now closed)

Poster session: REUSE YOUR OLD POSTER!
Sign up here and bring your old poster for another showing! Everyone is welcome to present, master students, PhDs, researchers and professors alike! There will be pizza, and maybe even a poster prize!

Keynote lecture:
Jennifer Lippincott-Schwartz
Janelia Research Campus, Howard Hughes Medical Institute (HHMI), Ashburn, VA, USA

Title: COPII with ALG2 and ESCRTs control lysosome-dependent microautophagy of ER exit sites

ER exit sites (ERESs) are tubular outgrowths of endoplasmic reticulum (ER) that serve as the earliest station for protein sorting and export into the secretory pathway. How these structures respond to different cellular conditions remains unclear. Here, we report that ERESs undergo lysosome-dependent microautophagy when Ca2+ is released by lysosomes in response to nutrient stressors such as mTOR inhibition or amino acid starvation. The pathway occurred downstream of macroautophagy and involved LC3-labeled lysosomes. Once associated with such lysosomes, ERESs were encapsulated, internalized into intraluminal structures, and subsequently degraded. The mechanism underlying ERES microautophagy was ESCRT-dependent and required ubiquitinated Sec31, ALG2 and ALIX. Knockout of ALG2 or function-blocking mutations of ALIX prevented lysosomal engulfment of ERESs. ERES microautophagy could be reconstituted in vitro using lysosomal lipid mimicking vesicles and purified recombinant components. Together, our results describe a novel pathway involving ERESs for bulk turnover of secretory proteins under nutrient stress.

The event is open for all, sign up below!

If you have any questions about the event, let us know by sending an email: svein.stove@uib.no

We hope to see you there!