Different localization of lysosomal-associated membrane protein 1 (LAMP1) in mammalian cultured cell lines

Baba, Kosuke; Kuwada, Sara; Nakao, Ayaka; Li, Xuebing; Okuda, Naoaki; Nishida, Ai; Mitsuda, Satoshi; Fukuoka, Natsuki; Kakeya, Hideaki; Kataoka, Takao

doi:10.1007/s00418-019-01842-z

Cited by 17 publications

(21 citation statements)

References 48 publications

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“…Importantly, other clues to the mechanisms responsible for CaMKII-dependent spectrin loss may be found in the confocal imaging studies of β IV -spectrin localization. Specifically, phosphomimetic and WT β IV -spectrin stimulated with AngII showed significant punctate patterns of localization (Fig 4F and 5D), consistent with those for both proteosomal complexes and/or lysosomal bodies (51,52). Notably, these puncta were absent when expressing β IV -spectrin under non-degrading conditions such as phospho-ablated β IV -spectrin with AngII (Fig 5D ), highlighting a clear association with Ser2254 phosphorylation status, β IV -spectrin stability, and nuclear STAT3 accumulation.…”

Section: Discussionsupporting

confidence: 66%

Ca2+/calmodulin kinase II–dependent regulation of βIV-spectrin modulates cardiac fibroblast gene expression, proliferation, and contractility

Nassal

Patel

Unudurthi

et al. 2021

Journal of Biological Chemistry

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This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

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Section: Discussionsupporting

confidence: 66%

Ca2+/calmodulin kinase II–dependent regulation of βIV-spectrin modulates cardiac fibroblast gene expression, proliferation, and contractility

Nassal

Patel

Unudurthi

et al. 2021

Journal of Biological Chemistry

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“…The copyright holder for this preprint this version posted December 11, 2020. ; https://doi.org/10.1101/2020.12.10.420711 doi: bioRxiv preprint reported to localize in the late endosomes (LEs), apart from their primary localization at the lysosomal compartments [58][59][60] . This finding indicates that colocalization of UL32-GFP-positive vesicles with LAMP1 in infected fibroblasts may derive from either LEs or from the lysosomes.…”

Section: Ul32-gfp Containing Vesicles Are Marked By Lamp1 But Not Lc3b and Gm130 In Fibroblastsmentioning

confidence: 99%

Cell Type-Specific Biogenesis of Novel Vesicles Containing Viral Products in Human Cytomegalovirus Infection

Momtaz

Molina

Mlera

et al. 2021

J Virol

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Human cytomegalovirus (HCMV), while highly restricted for the human species, infects an diverse array of cell types in the host. Patterns of infection are dictated by the cell type infected, but cell type-specific factors and how they impact tropism for specific cell types is poorly understood. Previous studies in primary endothelial cells showed that HCMV infection induces large multivesicular-like bodies (MVBs) that incorporate viral products, including dense bodies (DBs) and virions. Here we define the nature of these large vesicles using a recombinant virus where UL32, encoding the pp150 tegument protein, is fused in frame with green fluorescent protein (GFP, TB40/E-UL32-GFP). In fibroblasts, UL32-GFP-positive vesicles were marked with classical markers of MVBs, including CD63 and lysobisphosphatidic acid (LBPA), both classical MVB markers, as well as the clathrin and LAMP1. Unexpectedly, UL32-GFP-positive vesicles in primary human microvascular endothelial cells (HMVECs) were not labeled by CD63, and LBPA was completely lost from infected cells. We defined these UL32-positive vesicles in endothelial cells using markers for the cis-Golgi (GM130), lysosome (LAMP1), and autophagy (LC3B). These findings suggest that UL32-GFP containing MVBs in fibroblasts are derived from the canonical endocytic pathway and takeover classical exosomal release pathway. However, UL32-GFP containing MVBs in HMVECs are derived from the early biosynthetic pathway and exploit a less characterized early Golgi-LAMP1-associated non- canonical secretory autophagy pathway. These results reveal striking cell-type specific membrane trafficking differences in host pathways that are exploited by HCMV, which may reflect distinct pathways for virus egress. Importance Human cytomegalovirus (HCMV) is a herpesvirus that, like all herpesvirus, that establishes a life-long infection. HCMV remains a significant cause of morbidity and mortality in the immunocompromised and HCMV seropositivity is associated with age-related pathology. HCMV infects many cells in the human host and the biology underlying the different patterns of infection in different cell types is poorly understood. Endothelial cells are important target of infection that contribute to hematogenous spread of the virus to tissues. Here we define striking differences in the biogenesis of large vesicles that incorporate virions in fibroblasts and endothelial cells. In fibroblasts, HCMV is incorporated into canonical MVBs derived from an endocytic pathway, whereas HCMV matures through vesicles derived from the biosynthetic pathway in endothelial cells. This work defines basic biological differences between these cell types that may impact how progeny virus is trafficked out of infected cells.

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“…Specifically, these mutants had decreased colocalisation with LAMP1, and increased colocalisation with LysoTracker compared to hWT. There are known to be some differences between LAMP1-positive compartments and LysoTrackerstained organelles 25 . Therefore, we speculate that LysoTracker may detect LAMP1-negative acidic vesicles.…”

Section: Discussionmentioning

confidence: 99%

Role of the EF-hand and coiled-coil domains of human Rab44 in localisation and organelle formation

Ogawa

Kadowaki

Tokuhisa

et al. 2020

Sci Rep

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Rab44 is a large Rab GTPase that contains an amino-terminal EF-hand domain, a coiled-coil domain, and a carboxyl-terminal Rab GTPase domain. However, the roles of the EF-hand and coiled-coil domains remain unclear. Here, we constructed various deletion and point mutants of human Rab44. When overexpressed in HeLa cells, the wild-type Rab44 (hWT) formed ring-like structures, and partially localised to lysosomes. The dominant negative mutant, hT847N, localised to lysosomes and the cytosol, while the constitutively active mutant, hQ892L, formed ring-like structures, and partially localised to the plasma membrane and nuclei. The hΔEF, hΔcoil, and h826-1021 mutants also formed ring-like structures; however, their localisation patterns differed from hWT. Analysis of live imaging with LysoTracker revealed that the size of LysoTracker-positive vesicles was altered by all other mutations than the hC1019A and hΔEF. Treatment with ionomycin, a Ca2+ ionophore, induced the translocation of hWT and hΔcoil into the plasma membrane and cytosol, but had no effect on the localisation of the hΔEF and h826-1021 mutants. Thus, the EF- hand domain is likely required for the partial translocation of Rab44 to the plasma membrane and cytosol following transient Ca2+ influx, and the coiled-coil domain appears to be important for localisation and organelle formation.

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Different localization of lysosomal-associated membrane protein 1 (LAMP1) in mammalian cultured cell lines

Cited by 17 publications

References 48 publications

Ca2+/calmodulin kinase II–dependent regulation of βIV-spectrin modulates cardiac fibroblast gene expression, proliferation, and contractility

Ca2+/calmodulin kinase II–dependent regulation of βIV-spectrin modulates cardiac fibroblast gene expression, proliferation, and contractility

Cell Type-Specific Biogenesis of Novel Vesicles Containing Viral Products in Human Cytomegalovirus Infection

Role of the EF-hand and coiled-coil domains of human Rab44 in localisation and organelle formation

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