Aleksandra (Sanya) Anisimova 's Avatar

Aleksandra (Sanya) Anisimova

@alessandrick.bsky.social

PhD student in molecular biology๐Ÿง‘โ€๐Ÿ”ฌ with great interest in ๐ŸงชRNA-binding proteins, โš—๏ธ ribosome, and ๐Ÿงฌgenome-wide approaches Dog trainer in the evenings and on the weekends ๐Ÿพ

32 Followers  |  34 Following  |  7 Posts  |  Joined: 02.04.2025  |  1.8944

Latest posts by alessandrick.bsky.social on Bluesky

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Ancestral P-body proteins rewired for autophagic recycling in the early land plant Marchantia polymorpha Processing bodies (P-bodies) are conserved ribonucleoprotein (RNP) granules central to RNA metabolism across eukaryotes. Although the mechanisms underlying their assembly are well understood, the path...

If youโ€™re enjoying some calm while others are on holiday, hereโ€™s a #NEW #preprint to dive into โ€” led by the brilliant @vbcscitraining.bsky.social student A. Abdrakhmanov:
๐Ÿ‘‡ A quick thread + link:
www.biorxiv.org/content/10.1...

11.08.2025 05:44 โ€” ๐Ÿ‘ 55    ๐Ÿ” 28    ๐Ÿ’ฌ 4    ๐Ÿ“Œ 3
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๐Ÿ“‘ New study! Why would cells invest in a protein that degrades within minutes? TRIM52 is one of the most unstable proteins in the human proteome. Research by @versteegga.bsky.social in Nature Communications reveals its advantageous role โžก๏ธ tinyurl.com/yw6wtzkc

@univie.ac.at
@meduniwien.ac.at

29.04.2025 13:04 โ€” ๐Ÿ‘ 13    ๐Ÿ” 4    ๐Ÿ’ฌ 0    ๐Ÿ“Œ 0

Huge thank you to our collaborators, Ameres @ameressl.bsky.social and Versteeg labs, for their essential input, insights, and support!

07.04.2025 19:57 โ€” ๐Ÿ‘ 1    ๐Ÿ” 0    ๐Ÿ’ฌ 0    ๐Ÿ“Œ 0

6/ ๐Ÿ“œ Check out the full study for details!
www.biorxiv.org/content/10.1...

@gekaragoz.bsky.social @maxperutzlabs.bsky.social @vbcscitraining.bsky.social
#RNA #UPR #ERstress #IGF2BP3 #RBP

07.04.2025 15:15 โ€” ๐Ÿ‘ 3    ๐Ÿ” 0    ๐Ÿ’ฌ 1    ๐Ÿ“Œ 0

5/ ๐Ÿฅ Why does this matter? The UPR is implicated in development and cancer - contexts where IGF2BP3 is highly expressed. This dual-layered regulatory mechanism may allow cells to shift between opposing IGF2BP3 functions, enabling cell state-specific fate decisions.

07.04.2025 15:13 โ€” ๐Ÿ‘ 1    ๐Ÿ” 0    ๐Ÿ’ฌ 1    ๐Ÿ“Œ 0
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4/ ๐Ÿ”ฌ Mechanistically, we observed increased association of IGF2BP3 with the mRNA decapping complex during ER stress, which can result in enhanced degradation of IGF2BP3 targets

07.04.2025 15:13 โ€” ๐Ÿ‘ 1    ๐Ÿ” 0    ๐Ÿ’ฌ 1    ๐Ÿ“Œ 0
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3/๐Ÿ“‰ By tracking changes in total and newly transcribed mRNAs, we show that IGF2BP3 facilitates UPR via two distinct mechanisms:
โ€ข It reduces protein folding load by destabilizing most of its target mRNAs
โ€ข It upregulates UPR effectors stabilizing mRNAs encoding select transcriptional regulators

07.04.2025 15:12 โ€” ๐Ÿ‘ 1    ๐Ÿ” 0    ๐Ÿ’ฌ 1    ๐Ÿ“Œ 0
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2/๐Ÿ”ฌ IGF2BP3 is an RNA-binding protein known for regulating mRNA stability, particularly in development & cancer. Surprisingly, under ER stress, IGF2BP3 binds key UPR effector transcripts including XBP1, HSPA5, and DDIT3 (CHOP) โ€”major regulators of ER stress adaptation & apoptosis

07.04.2025 15:10 โ€” ๐Ÿ‘ 1    ๐Ÿ” 0    ๐Ÿ’ฌ 1    ๐Ÿ“Œ 0
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1/ Thrilled to share the core of my PhD projectโ€”just posted on BioRxiv!๐Ÿšจ We uncover a novel role for IGF2BP3 in regulating the cellular response to the endoplasmic reticulum (ER) stress โ€“ the unfolded protein response (UPR). Thread ๐Ÿงต (1/6) โฌ‡๏ธ
www.biorxiv.org/content/10.1...

07.04.2025 15:09 โ€” ๐Ÿ‘ 34    ๐Ÿ” 8    ๐Ÿ’ฌ 2    ๐Ÿ“Œ 2

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