JM4 is a four‐transmembrane protein binding to the CCR5 receptor

Schweneker, Marc; Bachmann, André S.; Moelling, Karin

doi:10.1016/j.febslet.2005.02.037

Cited by 46 publications

(67 citation statements)

References 37 publications

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“…Mouse PRA1 export from the ER to the Golgi was shown to depend on homodimerization (Liang et al, 2004). The PRA1 domain-containing protein Jena-Muenchen 4 (JM4) forms a multimeric complex (Schweneker et al, 2005). We have observed homodimerization and heterodimerization among members of the AtPRA1 family.…”

Section: Discussionmentioning

confidence: 74%

“…This is not the first time that a PRA1 protein was found simultaneously in different compartments within the same cell. The human PRA1 domain-containing protein JM4 is present in the trans-Golgi, endosomes, and ER (Schweneker et al, 2005). In yeast, Yip3p was found in COPII vesicles through mass spectrometry (Otte et al, 2001), while rat PRA1 was identified in Golgi and COPI vesicles (Gilchrist et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

“…In human, yeast, and mouse, PRA1 resides predominantly in the Golgi apparatus (Liang and Li, 2000;Huh et al, 2003;Sivars et al, 2003). However, PRA1 proteins have been reported in different trafficking compartments, such as the ER (Abdul-Ghani et al, 2001;Schweneker et al, 2005;Liu et al, 2006), synaptic vesicles (Fenster et al, 2000), COPI and COPII vesicles (Otte et al, 2001;Gilchrist et al, 2006), and endosomes (Schweneker et al, 2005;Geerts et al, 2007). To determine the subcellular localization of the 19 AtPRA1 proteins, their full-length open reading frames were fused to the enhanced GFP reporter protein (EGFP) and stably produced in Arabidopsis seedlings.…”

Section: Subcellular Localization Of the Atpra1 Proteins In Arabidopsismentioning

confidence: 99%

“…Animal PRA1 proteins have been shown to function either as monomers or through the formation of a multimeric complex (Liang et al, 2004;Schweneker et al, 2005). To test whether all AtPRA1 proteins might interact to form dimers, yeast two-hybrid-based interaction analyses were carried out.…”

Section: Atpra1 Proteins Can Dimerize In Accordance With Their Phylogmentioning

confidence: 99%

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ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

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Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/ prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.

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Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Subcellular Localization Of the Atpra1 Proteins In Arabidopsismentioning

confidence: 99%

Section: Atpra1 Proteins Can Dimerize In Accordance With Their Phylogmentioning

confidence: 99%

See 2 more Smart Citations

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…Several JWA homologues (e.g., ARL-6, GTRAP3-18, addicsin and JM4) were since identified (Butchbach et al, 2002;Schweneker et al, 2005). These homologues contain a large prenylated Rab acceptor 1 domain, believed to form a new family of ADP-ribosylation factor proteins that has a role in the regulation of intracellular protein transport (Ingley et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

JWA regulates melanoma metastasis by integrin αVβ3 signaling

Bai

Zhang

et al. 2009

Oncogene

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JWA, a newly identified novel microtubule-associated protein (MAP), was recently demonstrated to be indispensable for the rearrangement of actin cytoskeleton and activation of MAPK cascades induced by arsenic trioxide (As 2 O 3 ) and phorbol ester (PMA). JWA depletion blocked the inhibitory effect of As 2 O 3 on HeLa cell migration, but enhanced cell migration after PMA treatment. As cancer cell migration is a hallmark of tumor metastasis and the functional role of JWA in cancer metastasis is not understood, here we show that JWA has an important role in melanoma metastasis. Our data demonstrated that JWA knockdown increased the adhesion and invasion abilities of melanoma cells. Furthermore, JWA knockdown in B16-F10 and A375 melanoma cells significantly promoted the formation and growth of metastatic colonies in vivo. Moreover, in the tumor biopsies from human melanoma patients, JWA expression was significantly decreased in malignant melanoma compared with normal nevi. In addition, we found that JWA knockdown could intensify tumor integrin a V b 3 signaling by regulating nuclear factor Sp1. These findings suggest that JWA suppresses melanoma metastasis and may serve a potential therapeutic target for human melanoma.

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Downregulation of JWA promotes tumor invasion and predicts poor prognosis in human hepatocellular carcinoma

Chen

Gao

et al. 2012

Mol. Carcinog.

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We previously identified JWA as a novel microtubule-associated protein (MAP), which is implicated in carcinogenesis and tumor progression. The aims of the present study were to investigate the biological action and the prognostic significance of JWA in hepatocellular carcinoma (HCC). Quantitative real-time PCR and Western blot were used to detect JWA mRNA and protein expression, respectively, in stepwise metastatic HCC cell lines and HCC tissues. Short hairpin RNA was used to inhibit JWA expression in HCC cells. The effects of JWA depletion on cell migration, invasion, adhesion and in vivo metastasis were investigated. Immunohistochemistry of JWA was conducted in microarrays with tissue from 314 HCC patients who had undergone surgical resection. Prognostic significance was assessed using the Kaplan-Meier method and log-rank tests. The result showed JWA expression was decreased in the highly metastatic HCC cell lines and HCC tissues. Depletion of JWA caused a notable increase in cell migration, invasion and adhesion in vitro and metastasis in vivo. Furthermore, there was an inverse correlation between JWA expression and FAK expression and phosphorylation, RhoA activation and matrix metalloproteinase-2 (MMP-2) activity in HCC cells. More notably, multivariate analysis revealed that a low level of JWA expression was an independent prognosticator for both recurrence-free and overall survival for HCC patients after surgical resection, especially for AFP-normal HCC patients. Taken together, our data demonstrate that JWA plays a crucial role in HCC progression and suggest JWA may be a potential prognostic biomarker and therapeutic target for HCC.

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JM4 is a four‐transmembrane protein binding to the CCR5 receptor

Cited by 46 publications

References 37 publications

ThePRA1Gene Family in Arabidopsis

ThePRA1Gene Family in Arabidopsis

JWA regulates melanoma metastasis by integrin αVβ3 signaling

Downregulation of JWA promotes tumor invasion and predicts poor prognosis in human hepatocellular carcinoma

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