Immunomodulatory drugs activate NK cells via both Zap-70 and cereblon-dependent pathways.


Journal

Leukemia
ISSN: 1476-5551
Titre abrégé: Leukemia
Pays: England
ID NLM: 8704895

Informations de publication

Date de publication:
01 2021
Historique:
received: 05 11 2019
accepted: 18 03 2020
revised: 17 03 2020
pubmed: 3 4 2020
medline: 14 1 2021
entrez: 3 4 2020
Statut: ppublish

Résumé

Immunomodulatory drugs (IMiDs) lenalidomide and pomalidomide show remarkable antitumor activity in multiple myeloma (MM) via directly inhibiting MM-cell growth in the bone marrow (BM) microenvironment and promoting immune effector cell function. They are known to bind to the ubiquitin 3 ligase CRBN complex and thereby triggering degradation of IKZF1/3. In this study, we demonstrate that IMiDs also directly bind and activate zeta-chain-associated protein kinase-70 (Zap-70) via its tyrosine residue phosphorylation in T cells. IMiDs also triggered phosphorylation of Zap-70 in natural killer (NK) cells. Importantly, increased granzyme-B (GZM-B) expression and NK-cell activity triggered by IMiDs is associated with Zap-70 activation and inhibited by Zap-70 knockdown (KD), independent of CRBN. We also demonstrate a second mechanism whereby IMiDs trigger GZM-B and NK cytotoxicity which is CRBN and IKZF3 mediated, and inhibited or enhanced by KD of CRBN or IKZF3, respectively, independent of Zap-70. Our studies therefore show that IMiDs can enhance NK and T-cell cytotoxicity in (1) ZAP-70-mediated CRBN independent, as well as (2) CRBN-mediated ZAP-70 independent mechanisms; and provide the framework for developing novel therapeutics to activate Zap-70 and thereby enhance T and NK anti-MM cytotoxicity.

Identifiants

pubmed: 32238854
doi: 10.1038/s41375-020-0809-x
pii: 10.1038/s41375-020-0809-x
pmc: PMC7529681
mid: NIHMS1578112
doi:

Substances chimiques

Adaptor Proteins, Signal Transducing 0
CRBN protein, human 0
Immunologic Factors 0
Ubiquitin-Protein Ligases EC 2.3.2.27
ZAP-70 Protein-Tyrosine Kinase EC 2.7.10.2
ZAP70 protein, human EC 2.7.10.2

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

177-188

Subventions

Organisme : NCI NIH HHS
ID : P01 CA155258
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA050947
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA178264
Pays : United States
Organisme : NCI NIH HHS
ID : P50 CA100707
Pays : United States

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Auteurs

Teru Hideshima (T)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA.

Daisuke Ogiya (D)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA.

Jiye Liu (J)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA.

Takeshi Harada (T)

Department of Medicine and Bioregulatory Sciences, University of Tokushima Graduate School of Medicine, 3-18-15 Kuramoto, Tokushima, 770-8503, Japan.

Keiji Kurata (K)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA.

Jooeun Bae (J)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA.

Walter Massefski (W)

Department of Chemistry Instrumentation Facility, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.

Kenneth C Anderson (KC)

Jerome Lipper Multiple Myeloma Center, Department of Medical Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA, 02215, USA. kenneth_anderson@dfci.harvard.edu.

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Classifications MeSH