Pooled overexpression screening identifies PIPPI as a novel microprotein involved in the ER stress response

Lorenzo Lafranchi1,2, Glancis Luzeena Raja1,2, Alberto M Arenas1,2

  • 1Science for Life Laboratory, Karolinska Institutet, Department of Medical Biochemistry and Biophysics, Division of Genome Biology, Solna 17165, Sweden.

Nucleic Acids Research
|November 8, 2025
PubMed

Insights

Researchers identified functional microproteins using pooled overexpression screens. They discovered PIPPI, a microprotein that protects cells from endoplasmic reticulum stress and modulates protein folding responses.

Area of Science:

  • Molecular Biology
  • Proteomics
  • Cell Biology

Background:

  • Microproteins encoded by short open reading frames (sORFs) are abundant but largely uncharacterized.
  • Understanding the function of these microproteins is crucial for deciphering the eukaryotic proteome.

Purpose of the Study:

  • To identify functional microproteins from a large library of sORFs.
  • To characterize the role of newly identified microproteins in cellular stress responses.

Main Methods:

  • Utilized pooled overexpression screens with a library of 11,338 sORFs.
  • Performed phenotypic screens to identify sORFs conferring resistance to 6-thioguanine.
  • Investigated the function and interactions of identified microproteins using molecular and cellular assays.

Main Results:

  • Identified two cytoprotective microproteins: altDDIT3 and PIPPI.
  • PIPpi, encoded within the LCR16a duplicon, modulates endoplasmic reticulum (ER) protein folding stress.
  • PIPpi interacts with ERp44 and protects cells from ER stress upon overexpression, while knockdown sensitizes cells.

Conclusions:

  • Pooled overexpression screens are effective for discovering functional microproteins.
  • PIPpi represents a novel microprotein involved in ER stress response pathways.
  • This study expands the functional annotation of the eukaryotic proteome through microprotein discovery.

Related Concept Videos

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
2.9K
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
6.2K
piRNA - Piwi-interacting RNAs02:57

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while only 2000 genes have been found for miRNAs. piRNAs can act at the transcriptional and post-transcriptional levels and have a vital role in silencing transposable elements present in germ cells. They are also involved in epigenetic silencing and activation. Previously, they were thought to function only in germ cells but new evidence suggests...
7.5K
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
10.0K