Identification of Tim4 as a phosphatidylserine receptor

By Masanori Miyanishi, K. Tada, Masato Koike, Y. Uchiyama, T. Kitamura, S. Nagata. Nature, 2007

1,196 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/e85838f7f77bf31df8b366a2f1a9388aa5c09d57

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In Immunology

In Molecular Biology

In Physiology

Citations in the corpus

Biodistribution and Delivery Efficiency of Unmodified Tumor-Derived Exosomes (2014, background): “impact on exosome circulation times in vivo [71].”
Immunobiology of the TAM receptors (2008, background): “Given the dependence on phosphatidylserine of TAM receptor action during phagocytosis, it will be interesting to examine potential physical interaction between TAM receptors and the recently described direct phosphatidylserine receptors TIM4 (T-cell immunoglobulin domain and mucin domain protein 4”
SORTING IT OUT: REGULATION OF EXOSOME LOADING (2014, background): “Additionally, cells can use Tim4 and Tim1 as phosphatidylserine receptors for the engulfment of exosomes [102].”
Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013, neutral): “Signals are transmitted by either direct interaction between the vesicle membrane protein and the recipient membrane protein [2, 6] or by internalization of the vesicle content by the recipient cell [7–9].”
An Apoptotic 'Eat Me' Signal: Phosphatidylserine Exposure. (2015, methodology): “This procedure led to the identification of Tim4 (T cell immunoglobulin and mucin domain-containing molecule 4) [61], a type I membrane protein that is highly expressed in resident peritoneal macrophages.”
Membrane vesicles as conveyors of immune responses (2009, background): “For example, T cell immunoglobulin domain and mucin domain protein 1 ( TIM1 ; also known as HAVCR1) and TIM4 (also known as TIMD4), which have recently been described to be phosphatidylserine-binding molecules, are expressed on the surface of activated lymphocytes or phagocytes, respectively, and ”
Self-renewing resident cardiac macrophages limit adverse remodeling following myocardial infarction (2018, positive): “For instance, the phosphatidylserine receptor, TIMD4, is utilized by macrophages in efferocytosis 17 ; without which ischemic injury is amplified 31 .”
Routes and mechanisms of extracellular vesicle uptake (2014, background): “Incubation of macrophages with an antibody that masks TIM4, a receptor involved in PS-dependent phagocytosis (27,81), leads to reduced uptake of EVs (27).”
Common variants at 30 loci contribute to polygenic dyslipidemia (2008, background): “TIMD4 and HAVCR1 were recently identified as phosphatidylserine receptors on macrophages that facilitate the engulfment of apoptotic cell”
TIM genes: a family of cell surface phosphatidylserine receptors that regulate innate and adaptive immunity (2010, background): “In contrast, thioglycollate-elicited peritoneal macrophages lose TIM-4 expression and gain expression of TIM-3 and MFG-E8 (16, 18).”
Cellular Internalization of Exosomes Occurs Through Phagocytosis (2010, background): “identified TIM-4 and TIM-1 as endogenous phagocytic receptors for apoptotic cells (41).”