<i>Quo Vadis:</i> Polarized Membrane Recycling in Motility and Phagocytosis

Mellman, Ira

doi:10.1083/jcb.149.3.529

Cited by 25 publications

(17 citation statements)

References 15 publications

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“…Consistent with the central role of the Golgi complex in the secretory pathway (Lippincott-Schwartz et al, 1998;Donaldson and Lippincott-Schwartz, 2000;Lemmon and Traub, 2000;Mellman, 2000), STAMP2 is found in VST structures in the cytosol and colocalizes with EEA1, an early endosome marker (Stenmark et al, 1996). The significant STAMP2 distribution in the plasma membrane, and the movement of STAMP2 within transport vesicles to and from the plasma membrane in live-cell imaging studies suggest that STAMP2 may be involved in the secretory and endocytic pathways.…”

Section: Discussionmentioning

confidence: 56%

Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer

et al. 2005

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We have identified a novel gene, six transmembrane protein of prostate 2 (STAMP2), named for its high sequence similarity to the recently identified STAMP1 gene. STAMP2 displays a tissue-restricted expression with highest expression levels in placenta, lung, heart, and prostate and is predicted to code for a 459-amino acid six transmembrane protein. Using a form of STAMP2 labeled with green flourescent protein (GFP) in quantitative time-lapse and immunofluorescence confocal microscopy, we show that STAMP2 is primarily localized to the Golgi complex, trans-Golgi network, and the plasma membrane. STAMP2 also localizes to vesicular-tubular structures in the cytosol and colocalizes with the Early Endosome Antigen1 (EEA1) suggesting that it may be involved in the secretory/endocytic pathways. STAMP2 expression is exquisitely androgen regulated in the androgen-sensitive, androgen receptor-positive prostate cancer cell line LNCaP, but not in androgen receptornegative prostate cancer cell lines PC-3 and DU145. Analysis of STAMP2 expression in matched normal and tumor samples microdissected from prostate cancer specimens indicates that STAMP2 is overexpressed in prostate cancer cells compared with normal prostate epithelial cells. Furthermore, ectopic expression of STAMP2 in prostate cancer cells significantly increases cell growth and colony formation suggesting that STAMP2 may have a role in cell proliferation. Taken together, these data suggest that STAMP2 may contribute to the normal biology of the prostate cell, as well as prostate cancer progression.

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Section: Discussionmentioning

confidence: 56%

Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer

et al. 2005

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“…The transit through the recycling endosome proceeds with slower kinetics than the transport through early endosomes and appears to delay the rate of recycling, causing an accumulation of the intracellular pool of receptors and other plasma membrane components (61,63). MVBs are also presumed to function as sources of plasma membrane which are necessary for the formation of cellular protrusions during migration and phagocytosis (43). Thus, the forward margins of moving cells contain frequently recycling receptors, even those which are known to reside in recycling endosomes (e.g., the TfR [5,31,52]).…”

Section: Discussionmentioning

confidence: 99%

VP40, the Matrix Protein of Marburg Virus, Is Associated with Membranes of the Late Endosomal Compartment

Kolesnikova

Bugany

Klenk

et al. 2002

J Virol

130

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Localization of VP40 in Marburg virus (MBGV)-infected cells was studied by using immunofluorescence and immunoelectron microscopic analysis. VP40 was detected in association with nucleocapsid structures, present in viral inclusions and at sites of virus budding. Additionally, VP40 was identified in the foci of virus-induced membrane proliferation and in intracellular membrane clusters which had the appearance of multivesicular bodies (MVBs). VP40-containing MVBs were free of nucleocapsids. When analyzed by immunogold labeling, the concentration of VP40 in MVBs was six times higher than in nucleocapsid structures. Biochemical studies showed that recombinant VP40 represented a peripheral membrane protein that was stably associated with membranes by hydrophobic interaction. Recombinant VP40 was also found in association with membranes of MVBs and in filopodia-or lamellipodia-like protrusions at the cell surface. Antibodies against marker proteins of various cellular compartments showed that VP40-positive membranes contained Lamp-1 and the transferrin receptor, confirming that they belong to the late endosomal compartment. VP40-positive membranes were also associated with actin. Western blot analysis of purified MBGV structural proteins demonstrated trace amounts of actin, Lamp-1, and Rab11 (markers of recycling endosomes), while markers for other cellular compartments were absent. Our data indicate that MBGV VP40 was able to interact with membranes of late endosomes in the course of viral infection. This capability was independent of other MBGV proteins. The family of Filoviridae comprises Marburg virus (MBGV)and Ebola virus (EBOV), which cause a severe and often fatal hemorrhagic disease in human and nonhuman primates. During the reported outbreaks, up to 80% of the cases had a fatal outcome. The recent outbreak of MBGV hemorrhagic fever in the Democratic Republic of the Congo underlines the emerging potential of this pathogen (68). Filoviral infections are pantropic, affecting almost every organ of the infected host. However, the major and primary targets are cells of the mononuclear phagocytic system (55).The enveloped MBGV particles are composed of seven structural proteins and the nonsegmented negative-strand RNA genome (7,15). The viral envelope is spiked with homotrimers of the glycoprotein GP (1,16,60). Four proteins are components of the nucleocapsid: the nucleoprotein NP (2,36,40,57), the L protein (46), VP35 (45), and VP30 (2). NP, VP35, and L are essential for viral replication and transcription (45); the function of VP30, an NP-binding phosphoprotein, is still unclear (44).Between the nucleocapsid and the viral envelope, MBGV particles contain two proteins, VP24 and the highly abundant VP40, whose function is not yet elucidated (2, 13). However, the position of VP40 in the genome (third gene), its hydrophobicity, and its abundance within the virions suggest that VP40 represents a homologue of the matrix proteins of other nonsegmented negative-strand RNA viruses.It is currently believed that matrix prot...

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“…Recently, different studies have suggested that membrane traffic can contribute to regulate PM architecture, through the insertion and uptake of membrane at the PM (Bajno et al, 2000;Mellman, 2000;Palacios et al, 2001;Ridley, 2001). Arf6, a member of the ADP-ribosylation factor (ARF) family of GTPases is an important regulator of the PM architecture.…”

Section: Discussionmentioning

confidence: 99%

Alterations in the Arf6-regulated plasma membrane endosomal recycling pathway in cells overexpressing the tetraspan protein Gas3/PMP22

Chies

Nobbio

Edomi

et al. 2003

Journal of Cell Science

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Growth arrest specific 3 (Gas3)/peripheral myelin protein 22 (PMP22) is a component of the compact peripheral nerve myelin, and mutations affecting gas3/PMP22 gene are responsible for a group of peripheral neuropathies in humans. We have performed in vivo imaging in order to investigate in detail the phenotype induced by Gas3/PMP22 overexpression in cultured cells. Here we show that Gas3/PMP22 triggers the accumulation of vacuoles, before the induction of cell death or of changes in cell spreading. Overexpressed Gas3/PMP22 accumulates into two distinct types of intracellular membrane compartments. Gas3/PMP2 accumulates within late endosomes close to the juxtanuclear region, whereas in the proximity of the cell periphery, it induces the formation of actin/phosphatidylinositol (4,5)-bisphosphate(PIP2)-positive large vacuoles. Gas3/PMP22-induced vacuoles do not contain transferrin receptor, but instead they trap membrane proteins that normally traffic through the ADP-ribosylation factor 6 (Arf6) endosomal compartment. Arf6 and Arf6-Q67L co-localize with Gas3/PMP22 in these vacuoles,and the dominant negative mutant of Arf6, T27N, blocks the appearance of vacuoles in response to Gas3/PMP22, but not its accumulation in the late endosomes. Finally a point mutant of Gas3/PMP22 responsible for the Charcot-Marie-Tooth 1A disease is unable to trigger the accumulation of PIP2-positive vacuoles. Altogether these results suggest that increased Gas3/PMP22 levels can alter membrane traffic of the Arf6 plasma-membrane–endosomal recycling pathway and show that, similarly to other tetraspan proteins, Gas3/PMP22 can accumulate in the late endosomes.

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Quo Vadis: Polarized Membrane Recycling in Motility and Phagocytosis

Cited by 25 publications

References 15 publications

Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer

Molecular cloning and characterization of STAMP2, an androgen-regulated six transmembrane protein that is overexpressed in prostate cancer

VP40, the Matrix Protein of Marburg Virus, Is Associated with Membranes of the Late Endosomal Compartment

Alterations in the Arf6-regulated plasma membrane endosomal recycling pathway in cells overexpressing the tetraspan protein Gas3/PMP22

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