Ayala Shiber

Ayala Shiber

Education/ Resume:


2009 -2014 Ph.D., Biochemistry, The Hebrew University of Jerusalem, Israel.
Thesis: “The role of cellular chaperones in the degradation of misfolded proteins by the ubiquitin-proteasome system” Advisor: Prof. Tommer Ravid.

2004 – 2006 M.Sc., Genetics; Ben Gurion University of the Negev, Beer Sheva, Israel
Thesis: “The role of the Cs-ACS1G gene, the Female locus of cucumber in floral dimorphism”. Advisor: Dr. Tova Trebitsh.

2001 – 2004 B.Sc., Bio-Technological Engineering; Ben Gurion University of the Negev, Beer Sheva, Israel. Thesis: “Analysis of the Arabidopsis` Biotin Synthase (BIO-2) promoter’s expression pattern in tomato”Advisor: Dr. Orna Livneh.


2019-Present, Assistant Professor and Senior lecture
Faculty of Biology, Technion, Israel Institute of Technology, Israel
Research in the field of co-translational protein folding, assembly and quality control pathways, in health and disease.

2014-2019, Postdoctoral research fellow
Heidelberg University; The center for molecular biology (ZMBH) and the German Cancer Research Center (DKFZ), Heidelberg, Germany.
Research in the field of mRNA translation, ribosome associated factors and protein biogenesis.Prof. Dr. Bernd Bukau research group.


2006 – 2009, Manager of the DNA markers development unit, Bio-Technology Laboratories, Research & Development division, Hazera Genetics Inc., Kiryat Gat, Israel. Leading multiple projects in the field of quantitative genetics aiming at development and implementation of advanced technologies for producing genomic based breeding pipelines, including genotyping technologies, association studies, gene discovery and quantitative genetics analysis strategies.

2003 – 2004, Research assistant (Student position, in the last year of B.Sc. studies), BioTechnology Laboratories, Research & Development division, Hazera Genetics Inc., Kiryat Gat, Israel.

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Research Summary

Folding and misfolding on the ribosome:
Co-translational protein folding, assembly and quality control, in health and disease
The majority of cellular proteins do not function alone; they often act together in complexes to achieve concerted functions.

Despite the prevalence of protein complexes, very little is known of the mechanisms that ensure their correct folding and assembly.
The importance of the folding and assembly challenge is underscored by the growing number of misfolding diseases, such as Alzheimer’s and Parkinson’s. All of which are characterized by the accumulation of misfolded proteins in aggregates.

Here we study how do proteins form, fold and assemble into functional complexes in our cells, what mechanisms facilitate and protect them from aggregation, neurodegeneration, and aging.

Our key questions are:

  • How are nanomachines formed in our cells?
  • How do ribosomes go beyond synthesis to direct the polypeptide-chain folding and assembly?
  • How do “lonely” proteins find their complex and pathway partners?
  • What co-translational mechanisms protect them from misfolding?
  • What co-translational mechanisms degrade “lonely” proteins?
  • Do mRNA subcellular organization facilitate complex assembly?

The lab combines a variety of approaches including:
Advanced genetics (Next- Generation Sequencing), Biochemistry and Cell biology, using the awesome power of yeast as a model organism as well as cell culture.
The lab combines a variety of highly advanced methodologies including:

  • Selective Ribosome Profiling – capturing the ribosomes engaged by target proteins, in codon resolution
  • Single-molecule Fluorescence in situ hybridization (FISH) for imaging mRNAs in the cell
  • Developing novel techniques for single-molecule capturing of protein-mRNA interactions


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“Oskar Davis American Technion Society” award for young group leaders (2020), “Alexander von Humboldt” research fellowship (2015-2017), FEBS Excellence award (2017), HUJI Scholarship for academic excellence (2009-2014), “Hazera genetics award” for industrial innovation (2009)

Key Publications
  • Shiber A., Döring K., Friedrich U., Klann K., Merker D., Zedan M., Tippmann F., Kramer G., Bukau B. “Co-translational assembly of protein complexes in eukaryotes revealed by ribosome profiling”. (2018) Nature. 561(7722):268-272.https://www.nature.com/articles/s41586-018-0462-y
    Shiber A. Co-corresponding author.
    Featured in Nature News and Views, 29 AUGUST 2018: “Protein complexes assemble as they are being made”. Mayr,C.
  • Shiber A., Ravid T. “Chaperoning Proteins for Destruction: Diverse Roles of Heat Shock Proteins in Targeting Misfolded Proteins to the Proteasome”. (2014) Biomolecules. 17;4(3):704-24.https://www.mdpi.com/2218-273X/4/3/704
  • Shiber A, Gaur RK, Rimon-Knopf R, Zelcer A, Trebitsh T. “The origin and mode of function of the Female locus in cucumber”. (2008) Cucurbitaceae. 2008:263–270https://w3.avignon.inra.fr › dspace › bitstream › 5_51_Trebitsh
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Open Positions

Looking for students for MSc, Ph.D. & Post-Docs
Wanted: curious and enthusiastic human beings to solve the great mysteries of life

  • How do proteins find love at the end of the ribosomal tunnel?
  • What happens when proteins get lonely?
  • How can we live forever?

Come help us figure out how do proteins form, fold and organize into functional complexes in our cells,

What mechanisms facilitate and protect them from aggregation, neurodegeneration, and aging

The Shiber lab is open and we`re looking for you

Further details


Ayala Shiber


Emerson Building, Room 3-26

Faculty of Biology, Technion

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