A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1

Lin, Ching Yi; Li, Chun Chun; Huang, Pei‐Hsin; Lee, Fang‐Jen S.

doi:10.1242/jcs.00123

Cited by 41 publications

(43 citation statements)

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our in vitro data indicate that ARA6 is the only non-ARF GP to undergo N-myristoylation in A. thaliana. Two nuclear ARLs, ARL4 and ARL5, are known to be myristoylated in animals (57,58). This situation contrasts with that in plants, in which none of the ARLs is myristoylated (Table II).…”

Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 92%

“…We did not expect to find that some TF were substrates of NMT and the functional significance of this result is unclear. Three nuclear proteins were recently shown to be N-myristoylated in yeast and humans (57,58,60). The role of MYR in nuclear proteins can be explained by several variations on a basic idea, as myristate is known to act in concert with other mechanisms in the regulation of protein targeting and function (61).…”

Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 99%

See 1 more Smart Citation

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Boisson¹,

Giglione

Meinnel

2003

Journal of Biological Chemistry

143

157

View full text Add to dashboard Cite

N-Myristoylation is an irreversible modification that affects the membrane binding properties of crucial cytoplasmic proteins from signal transduction cascades. We characterized the two putative N-myristoyltransferases of Arabidopsis thaliana as a means of investigating the entire N-myristoylation proteome (N-myristoylome) in a higher eukaryote. AtNMT1 compensated for the nmt1 defect in yeast, whereas AtNMT2 and chimeras of the two genes did not. Only AtNMT1 modified known N-myristoylated proteins in vitro. AtNMT1 is therefore responsible for the A. thaliana N-myristoylome, whereas AtNMT2 does not seem to have usual myristoylation activity. We began with the whole set of N-myristoylated G proteins in the A. thaliana proteome. We then used a reiterative approach, based on the in vitro N-myristoylation of more than 60 different polypeptides, to determine the substrate specificity of AtNMT1. We found that the positive charge on residue 7 of the substrate was particularly important in substrate recognition. The A. thaliana N-myristoylome consists of 437 proteins, accounting for 1.7% of the complete proteome. We demonstrated the N-myristoylation of several unexpected protein families, including innate immunity proteins, thioredoxins, components of the protein degradation pathway, transcription factors, and a crucial regulatory enzyme of glycolysis. The role of N-myristoylation is discussed in each case; in particular, this process may underlie the "guard" hypothesis of innate immunity.

show abstract

Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 92%

Section: Transduction Pathways Involve a Large Number Of N-myristoylamentioning

confidence: 99%

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Boisson¹,

Giglione

Meinnel

2003

Journal of Biological Chemistry

143

157

View full text Add to dashboard Cite

show abstract

“…The polyclonal antibodies against ARL4A, ARL4C and ARL4D used in this study have been previously described (Lin et al, 2002;Li et al, 2007). The polyclonal antibody against GCC185 was developed by immunizing rabbits with a purified recombinant His-tagged GCC185 fragment (residues 414-733).…”

Section: Antibodiesmentioning

confidence: 99%

“…Among the more than 20 members of the ARL family in mammals, the expression levels of the three isoforms of ARL4 (i.e. ARL4A, ARL4C, ARL4D) are developmentally regulated, tissue specific and dependent on the stages of differentiation (Schürmann et al, 1994;Stephan et al, 1999;Lin et al, 2000;Lin et al, 2002). Disruption of the ARL4A gene in mice reduces the sperm count; in particular, ARL4A is involved in the early stages of spermatogenesis in adults (Schürmann et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

ARL4A acts with GCC185 to modulate Golgi complex organization

Lin

Chiang

Liu

et al. 2011

Journal of Cell Science

Self Cite

View full text Add to dashboard Cite

Summary ADP-ribosylation factor-like protein 4A (ARL4A) is a developmentally regulated member of the ARF/ARL GTPase family. The primary structure of ARL4A is very similar to that of other ARF/ARL molecules, but its function remains unclear. The trans-Golgi network golgin GCC185 is required for maintenance of Golgi structure and distinct endosome-to-Golgi transport. We show here that GCC185 acts as a new effector for ARL4 to modulate Golgi organization. ARL4A directly interacts with GCC185 in a GTP-dependent manner. Sub-coiled-coil regions of the CC2 domain of GCC185 are required for the interaction between GCC185 and ARL4A. Depletion of ARL4A reproduces the GCC185-depleted phenotype, causing fragmentation of the Golgi compartment and defects in endosome-to-Golgi transport. GCC185 and ARL4A localize to the Golgi independently of each other. Deletion of the ARL4A-interacting region of GCC185 results in inability to maintain Golgi structure. Depletion of ARL4A impairs the interaction between GCC185 and cytoplasmic linker-associated proteins 1 and 2 (CLASP1 and CLASP2, hereafter CLASPs) in vivo, and abolishes the GCC185-mediated Golgi recruitment of these CLASPs, which is crucial for the maintenance of Golgi structure. In summary, we suggest that ARL4A alters the integrity of the Golgi structure by facilitating the interaction of GCC185 with CLASPs.

show abstract

“…ARL1 and ARL3 have recently been shown to be required for localization of GRIP-domain proteins to Golgi membranes (Lowe, 1996;Lu, 2001;Panic, 2003;Setty, 2003). In addition, the expression of ARL4 and ARL5 was found to be developmentally regulated (Lin, 2000;Lin, 2002;Schurmann, 2002). These observations suggest the possibility that the ARL proteins function in membrane traffic which might mediate some developmental processes.…”

mentioning

confidence: 93%

Expression of ADP-ribosylation factor (ARF)-like protein 6 during mouse embryonic development

Takada¹,

Iida²,

Sasaki³

et al. 2005

Int. J. Dev. Biol.

View full text Add to dashboard Cite

ADP-ribosylation factor (ARF)-like protein 6 (ARL6) is a member of the ARF-like protein (ARL) subfamily of small GTPases (Moss, 1995; Chavrier, 1999). ARLs are highly conserved through evolution and most of them possess the consensus sequence required for GTP binding and hydrolysis (Pasquallato, 2002). Among ARLs, ARL6 which was initially isolated from a J2E erythroleukemic cell line is divergent in its consensus sequences and its expression has been shown to be limited to the brain and kidney in adult mouse (Ingley, 1999). Recently, it was reported that mutations of the ARL6 gene cause type 3 Bardet-Biedl syndrome in humans and that ARL6 is involved in ciliary transport in C. elegans (Chiang, 2004;Fan, 2004). Here, we investigated the expression pattern of ARL6 during early mouse development by whole-mount in situ hybridization and found that interestingly, ARL6 mRNA was localized around the node at 7.0-7.5 days post coitum (dpc) embryos, while weak expression was also found in the ectoderm. At the later stage (8.5 dpc) ARL6 was expressed in the neural plate and probably in the somites. Based on these results, a possible role of ARL6 in early development is discussed in relation to the findings in human and C. elegans (Chiang, 2004;Fan, 2004 (Moss, 1995;Chavrier, 1999). Although ARF-like proteins (ARLs) are very similar to ARFs in amino acid sequences, their biological function remains unclear. ARL1 and ARL3 have recently been shown to be required for localization of GRIP-domain proteins to Golgi membranes (Lowe, 1996;Lu, 2001;Panic, 2003;Setty, 2003). In addition, the expression of ARL4 and ARL5 was found to be developmentally regulated (Lin, 2000;Lin, 2002;Schurmann, 2002). These observations suggest the possibility that the ARL proteins function in membrane traffic which might mediate some developmental processes. ARL6 was first identified in a J2E erythroleukemic cell line. The ARL6 transcript is up-regulated during erythropoietin-induced differentiation of erythroid cells and down-regulated during interleukin-6-induced macrophage differentiation, suggesting a possible role in hemopoietic development (Ingley, 1999). In adult mice, ARL6 shows a tissue-specific expression pattern with the highest expression observed in the brain and kidney. In addition, yeast two-hybrid screening and coimmunoprecipitation reportedly show that ARL6 interacts with the protein-conducting channel subunit SEC61β (Ingley, 1999; Int. J. Dev. Biol. 49: 891-894 (2005) Pettersson, 2000). However, its biological functions remain unclear. Recently, ARL6 was identified as the gene that causes Bardet-Biedl syndrome type 3 (BBS3) (Chiang, 2004;Fan, 2004). Four different homozygous substitutions in the regions including the GTP binding domain in ARL6 were found to be involved in BBS3. BBS3 is a multisystemic disorder characterized by obesity, blindness, polydactyly, renal abnormalities and cognitive impairment. Similar to other BBS's, BBS3 is also thought to result from ciliary dysfunction because loss-of-function mutations ...

show abstract

A developmentally regulated ARF-like 5 protein (ARL5), localized to nuclei and nucleoli, interacts with heterochromatin protein 1

Cited by 41 publications

References 58 publications

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

Unexpected Protein Families Including Cell Defense Components Feature in the N-Myristoylome of a Higher Eukaryote

ARL4A acts with GCC185 to modulate Golgi complex organization

Expression of ADP-ribosylation factor (ARF)-like protein 6 during mouse embryonic development

Contact Info

Product

Resources

About