The Morin group works towards developing proteomic methods for protein function research and the global analysis of post-translational modifications (e.g., phospho, ubiquitin, methyl, acetyl) with expertise is in advanced proteomics methods, biochemistry and RNA processing. The research focuses on understanding the function of somatically mutated cancer genes, with an emphasis on proteins involved in the regulation of alternative splicing. Dr. Morin’s group also develops proteomic methods for ultra high proteome coverage and quantification of fresh-frozen paraffin-embedded (FFPE) tumour sections.



We are located at Canada's Michael Smith Genome Sciences Centre, part of the BC Cancer Research Centre.

675 West 10th Avenue 
Vancouver, British Columbia 
V5Z 1L3 


Selected Publications

Proteomic analysis of archival breast cancer clinical specimens identifies biological subtypes with distinct survival outcomes

Nature Communications
Karama Asleh, Gian Luca Negri, Sandra E Spencer Miko, Shane Colborne, Christopher S Hughes, Xiu Q Wang, Dongxia Gao, C Blake Gilks, Stephen KL Chia, Torsten O Nielsen, Gregg B Morin

Despite advances in genomic classification of breast cancer, current clinical tests and treatment decisions are commonly based on protein level information. Formalin-fixed paraffin-embedded (FFPE) tissue specimens with extended clinical outcomes are widely available. Here, we perform comprehensive proteomic profiling of 300 FFPE breast cancer surgical specimens, 75 of each PAM50 subtype, from patients diagnosed in 2008-2013 (n = 178) and 1986-1992 (n = 122) with linked clinical outcomes. These two cohorts are analyzed separately, and we quantify 4214 proteins across all 300 samples. Within the aggressive PAM50-classified basal-like cases, proteomic profiling reveals two groups with one having characteristic immune hot expression features and highly favorable survival. Her2-Enriched cases separate into heterogeneous groups differing by extracellular matrix, lipid metabolism, and immune-response features. Within 88 triple-negative breast cancers, four proteomic clusters display features of basal-immune hot, basal-immune cold, mesenchymal, and luminal with disparate survival outcomes. Our proteomic analysis characterizes the heterogeneity of breast cancer in a clinically-applicable manner, identifies potential biomarkers and therapeutic targets, and provides a resource for clinical breast cancer classification.

Characterization of a small molecule inhibitor of disulfide reductases that induces oxidative stress and lethality in lung cancer cells

Cell Reports
Fraser D Johnson, et al. (including Gregg B Morin).

Phenotype-based screening can identify small molecules that elicit a desired cellular response, but additional approaches are required to characterize their targets and mechanisms of action. Here, we show that a compound termed LCS3, which selectively impairs the growth of human lung adenocarcinoma (LUAD) cells, induces oxidative stress. To identify the target that mediates this effect, we use thermal proteome profiling (TPP) and uncover the disulfide reductases GSR and TXNRD1 as targets. We confirm through enzymatic assays that LCS3 inhibits disulfide reductase activity through a reversible, uncompetitive mechanism. Further, we demonstrate that LCS3-sensitive LUAD cells are sensitive to the synergistic inhibition of glutathione and thioredoxin pathways. Lastly, a genome-wide CRISPR knockout screen identifies NQO1 loss as a mechanism of LCS3 resistance. This work highlights the ability of TPP to uncover targets of small molecules identified by high-throughput screens and demonstrates the potential therapeutic utility of inhibiting disulfide reductases in LUAD.

De novo and cell line models of human mammary cell transformation reveal an essential role for Yb-1 in multiple stages of human breast cancer

Cell Death and Differentiation
Sylvain Lefort, Amal El-Naggar, Susanna Tan, Shane Colborne, Gian Luca Negri, Davide Pellacani, Martin Hirst, Barry Gusterson, Gregg B Morin, Poul H Sorensen, Connie J Eaves

Breast cancer heterogeneity has made it challenging to identify mechanisms critical to the initial stages of their genesis in vivo. Here, we sought to interrogate the role of YB-1 in newly arising human breast cancers as well as in established cell lines. In a first series of experiments, we found that short-hairpin RNA-mediated knockdown of YB-1 in MDA-MB-231 cells blocked both their local tumour-forming and lung-colonising activity in immunodeficient mice. Conversely, upregulated expression of YB-1 enhanced the poor in vivo tumorigenicity of T47D cells. We then found that YB-1 knockdown also inhibits the initial generation in mice of invasive ductal carcinomas and ductal carcinomas in situ from freshly isolated human mammary cells transduced, respectively, with KRASG12D or myristoylated-AKT1. Interestingly, increased expression of HIF1α and G3BP1, two YB-1 translational targets and elements of a stress-adaptive programme, mirrored the levels of YB-1 in both transformed primary and established MDA-MB-231 breast cancer cells.

Loss of m1acp3Ψ Ribosomal RNA Modification Is a Major Feature of Cancer

Cell Reports
Artem Babaian, Katharina Rothe, Dylan Girodat, Igor Minia, Sara Djondovic, Miha Milek, Sandra E Spencer Miko, Hans-Joachim Wieden, Markus Landthaler, Gregg B Morin, Dixie L Mager

The ribosome is an RNA-protein complex that is essential for translation in all domains of life. The structural and catalytic core of the ribosome is its ribosomal RNA (rRNA). While mutations in ribosomal protein (RP) genes are known drivers of oncogenesis, oncogenic rRNA variants have remained elusive. We identify a cancer-specific single-nucleotide variation in 18S rRNA at nucleotide 1248.U in up to 45.9% of patients with colorectal carcinoma (CRC) and present across >22 cancer types. This is the site of a unique hyper-modified base, 1-methyl-3-α-amino-α-carboxyl-propyl pseudouridine (m1acp3Ψ), a >1-billion-years-conserved RNA modification at the peptidyl decoding site of the ribosome. A subset of CRC tumors we call hypo-m1acp3Ψ shows sub-stoichiometric m1acp3Ψ modification, unlike normal control tissues. An m1acp3Ψ knockout model and hypo-m1acp3Ψ patient tumors share a translational signature characterized by highly abundant ribosomal proteins. Thus, m1acp3Ψ-deficient rRNA forms an uncharacterized class of “onco-ribosome” which may serve as a chemotherapeutic target for treating cancer patients.


Dr. Christopher Hughes

Mass Spectrometry Service Specialist

Dr. Grace Cheng

Staff Scientist

Dr. Gian Luca Negri

Staff Scientist

Postdoctoral Fellows

Dr. Brian Mooney

Postdoctoral Fellow


Richard Chen

Graduate Student

Ryan Riley

Graduate Student

Xander Yin

Graduate Student

Caitlyn De Jong

Graduate Student

Jenny Zhong

Graduate Student

Yueyang Li

Graduate Student

Siyu Miao

Graduate Student

Jiahua Tan

Graduate Student

Open Positions

Research Assistant 2 - Proteomics


Canada’s Michael Smith Genome Sciences Centre (GSC)

Today’s Research. Tomorrow’s Medicine.

The GSC is a department of the BC Cancer Research Institute and a high-throughput genome sequencing facility. We are leaders  in genomics, proteomics and bioinformatics in pursuit of novel treatment strategies for cancers and other diseases.

Among the world’s first genome centres to be established within a cancer clinic, for more than two decades our scientists and innovators have been designing and deploying cutting-edge technologies to benefit health and advance clinical research.

Among the GSC’s most significant accomplishments are the first  publication  to demonstrate the use of whole-genome sequencing to inform cancer treatment planning, the first published sequence of the SARS coronavirus genome and major contributions to the first physical map of the human genome as part of the Human Genome Project.

By joining the GSC you will become part of an exceptional and diverse team of scientists, clinicians, experts and professionals operating at the leading edge of clinical research. We look for people who share our core values—science, timeliness, respect—to join us on our mission to use genome science for the betterment of health and society.

Job Reference No. RA2_R00004_Proteomics_2024_06_03


The proteomics core facility at the Genome Sciences Centre assists a diverse base of collaborators and clients to characterize and quantify the changes in  the proteome that drive disease, particularly in cancer. Our work is multidisciplinary in nature, utilizing state-of-the-art mass spectrometry instrumentation and novel methodologies to identify and validate proteins that can act as therapeutic targets and biomarkers for the translation of genomic information into clinical practice.

The Research Assistant of the proteomics core facility will primarily be responsible for preparation of clinical and research samples for proteomic analysis. The position is within a multidisciplinary team that supports fostering scientific and personal development and learning within individuals and the group. The Research Assistant works together with the Facility Manager, staff scientists, and students to plan, coordinate, conduct and report on mass spectrometry based research projects. The successful candidate will have exemplary wet lab skills , organization, communication, and teamwork and be excited to work in a collaborative, multidisciplinary setting.



  • Maintaining data logs of samples analyzed and instrument use
  • Liaising with collaborators to coordinate sample submission and communicating results
  • Communicating and maintaining contact with client lab personnel
  • Maintaining a detailed lab notebook
  • Maintains and communicates inventory of laboratory supplies and equipment.


  • Preparing samples for proteomic analysis by following a variety of established technical procedures according to written protocols.
  • May operating facility instrumentation including off-line HPLC fractionation systems, mass spectrometers, speed vacs, and related instrumentation
  • Performing initial data analysis
  • May assist in the modification, development, and implementation of cutting edge protocols for clinical proteomics
  • Maintains and stores cell lines and primary cultures.
  • Maintains and stores test materials and products.
  • Assisting facility staff and collaborators with results dissemination.


  • Knowledge of tandem mass spectrometry and reversed phase chromatography (HPLC and nanoLC)
  • Experience in the handling of cells, tissues, and/or clinical samples
  • Practical experience with liquid chromatography, mass spectrometry instrumentation, proteomics sample preparation an asset

The applicant is expected to have a level of education, training, and experience equivalent to a BSc + 2 years of experience in an appropriate discipline or similar.


Every PHSA employee enables the best possible patient care for our patients and their families. Whether you are providing direct care, conducting research, or making it possible for others to do their work, you impact the lives of British Columbians today and in the future. That’s why we’re focused on your care too – offering health, wellness, development programs to support you – at work and at home.

  • Join one of BC’s largest employers with province-wide programs, services and operations – offering vast opportunities for growth, development, and recognition programs that honour the commitment and contribution of all employees.
  • Access to professional development opportunities through our in-house training programs, including +2,000 courses, such as our San’yas Indigenous Cultural Safety Training course, or Core Linx for Leadership roles.
  • Enjoy a comprehensive benefits package, which includes statutory benefits - Canada Pension Plan, Employment Insurance and WorkSafe BC plus the BC Cancer group benefits plan which includes medical & dental extended health, and group life insurance coverage, and psychological health & safety programs and holistic wellness resources.
  • Annual statutory holidays (13) with generous vacation entitlement and accruement.
  • PHSA is a remote work friendly employer, welcoming flexible work options to support our people (eligibility may vary, depending on position).
  • Access to WorkPerks, a premium discount program offering a wide range of local and national discounts on electronics, entertainment, dining, travel, wellness, apparel, and more.

Job Type

Temporary renewable, Full-Time, 7.5 hrs. per day

100% onsite

Salary Range

$57,347 to $75,268

The starting salary for this position would be determined with consideration of the successful candidate’s relevant education and experience, and would be in alignment with the provincial compensation reference plan. 


Please submit a detailed cover letter and resume to, using Job Reference No. RA2_R00004_Proteomics_2024_06_03 in the subject line of your email.

While we value and review all applications, please note that due to the volume of submissions only shortlisted candidates will be contacted. This posting will remain online until the position is filled.

All qualified candidates are encouraged to apply; however, Canadian citizens and permanent residents will be given priority.


As per the current Public Health Order, full vaccination against COVID-19 is a condition of employment with PHSA as of October 26, 2021.

Please note all jobs at the GSC are based in Vancouver, British Columbia, Canada. Flexible work options may be available for this position upon request and is subject to change in accordance with GSC’s operational needs and PHSA’s Flexible Work Options Policy.

We believe that equity, diversity and inclusivity are essential for the advancement of human knowledge and science.

We welcome all applicants and provide all employees with equal opportunity for advancement, regardless of race, colour, ancestry, place of origin, political belief, religion, marital status, family status, physical or mental disability, sex, sexual orientation, gender identity or expression, age, conviction of a criminal or summary conviction offence unrelated to their employment.

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