Journal
JOURNAL OF IMMUNOLOGY
Volume 204, Issue 5, Pages 1134-1145Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.1900671
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Funding
- National Natural Science Foundation of China [81770438, 91439122, 81473138]
- Major Research Program of Guangdong Science and Technology [2017A030308002, 2015B010109004]
- Academy of Finland [285223, 322647]
- Sigrid Juselius Foundation
- Academy of Finland (AKA) [322647, 322647] Funding Source: Academy of Finland (AKA)
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Phospholipase C (PLC) isoforms play central roles in signaling cascades by cleaving PIP2 into the second messengers IP3 and DAG. In this study, to our knowledge, we uncover that ORP5L interacts physically with PLC gamma 1 in T cells, extracts PIP2 from the plasma membrane via its ORD domain (OSBP-related domain), presents it to PLC gamma 1 (enabling IP3 generation), and eventually maintains intracellular Ca2+ homeostasis. Through this mechanism, ORP5L promotes T cell proliferation in a Ca2+-activated NFAT2-dependent manner. To our knowledge, our study uncovers a new key function of ORP5L as a critical cofactor for PLC gamma 1 catalysis and its crucial role in human T cell proliferation.
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