Expression Studies of CLN3 Protein (Battenin) in Fusion with the Green Fluorescent Protein in Mammalian Cellsin Vitro

Golabek, Adam A.; Kaczmarski, Wojciech; Kida, E; Kaczmarski, A.; Michalewski, Martin P.; Wisniewski, Krystyna E.

doi:10.1006/mgme.1999.2836

Cited by 34 publications

(29 citation statements)

References 14 publications

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“…For the bottom fraction, the signals for ER, mitochondria and MAT-DR were co-localized, possibly due to their co-precipitation. The density gradient pattern in Figure 3 was similar to the reported one for a CHO-K1 cell homogenate (Golabek et al 1999). Thus, the MAT-DR could be distributed in a limited region of the ER.…”

Section: Intracellular Localization Of Mat-drsupporting

confidence: 80%

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Stable expression and visualization of Mat-8 (FXYD-3) tagged with a fluorescent protein in Chinese Hamster Ovary (CHO)-K1 cells

2005

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A type I transmembrane protein, Mat-8 (FXYD-3), was tagged with fluorescent protein, Discosoma red fluorescent protein, at the carboxyl terminal cytoplasmic tail, and stably expressed in Chinese Hamster Ovary (CHO)-K1 cells. The fluorescence signal was distributed in intracellular membranes, being not only detected around the nuclear envelope but also partly overlapping with an endoplasmic reticulum marker. Subcellular fractionation by density gradient centrifugation supported this partial overlapping. The spherical structures observed were not colocalized with markers for lysosomes, endosomes, and Golgi bodies, suggesting that Mat-8 is distributed in a distinct endoplasmic reticulum region and the nuclear envelope after synthesis on membrane-bound ribosomes.

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Section: Intracellular Localization Of Mat-drsupporting

confidence: 80%

“…An aliquot (50 ll) was analyzed by Western blotting with antibodies for marker proteins such as PDI (ER), EEA1 (endosomes), and HSP70 (mitochondria and cytoplasm). In the lower panel, the distribution of marker proteins including those of lysosomes and Golgi bodies (Golabek et al 1999) is schematically shown. b 1995).…”

Section: Discussionmentioning

confidence: 99%

Stable expression and visualization of Mat-8 (FXYD-3) tagged with a fluorescent protein in Chinese Hamster Ovary (CHO)-K1 cells

2005

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“…Following the characterization of CLN3 topology, localization, and posttranslational modifications, protein interacting partners have been examined to determine the endogenous function of CLN3 (Table 1). CLN3 has been reported to be present in the nucleus [113], Golgi [114–116], mitochondria [117], plasma membrane [113], endosomes and lysosomes [114, 115, 118, 119], neuronal processes and synaptosomes [120, 121]. The localization experiments were conducted using several techniques and have been completed with different CLN3 antibodies, expression constructs, epitope tags, and cell types.…”

Section: Ncl-associated Membrane Proteinsmentioning

confidence: 99%

Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function

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Pearce

2010

Cell. Mol. Life Sci.

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Neuronal ceroid lipofuscinoses (NCL) are caused by mutations in eight different genes, are characterized by lysosomal accumulation of autofluorescent storage material, and result in a disease that causes degeneration of the central nervous system (CNS). Although functions are defined for some of the soluble proteins that are defective in NCL (cathepsin D, PPT1, and TPP1), the primary function of the other proteins defective in NCLs (CLN3, CLN5, CLN6, CLN7, and CLN8) remain poorly defined. Understanding the localization and network of interactions for these proteins can offer clues as to the function of the NCL proteins and also the pathways that will be disrupted in their absence. Here, we present a review of the current understanding of the localization, interactions, and function of the proteins associated with NCL.

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“…CLN3 has been demonstrated to be N-glycosylated (Jarvela et al, 1998;Golabek et al, 1999). Such a maturation of CLN3 would most likely occur in the ER or possibly the Golgi.…”

Section: Processing and Trafficking Of Cln3mentioning

confidence: 99%

“…A study by Golabek et al (1999) demonstrated that treatment with protease inhibitors decreased the formation of CLN3 in the lysosomal fraction, suggesting that CLN3 may undergo some sort of proteolytic modification. CLN3 is also phosphorylated .…”

Section: Processing and Trafficking Of Cln3mentioning

confidence: 99%

Localization and processing of CLN3, the protein associated to batten disease: Where is it and what does it do?

Pearce

2000

Journal of Neuroscience Research

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Although the CLN3 gene for Batten disease, the most common inherited neurovisceral storage disease of childhood, was identified in 1995, the function of the corresponding protein still remains elusive. A key to understanding the pathology of this devastating disease will be to elucidate the function of CLN3 at the molecular level. CLN3 has proven difficult to study, as it is predicted to be a membrane protein, and is of apparently low abundance in cells. Different groups have reported differing subcellular localization of CLN3. The purpose of this review is to critically examine the various cell biological approaches undertaken to localize CLN3 and to piece together a potential function for CLN3 in neuronal cells. The most likely conclusion of this is that CLN3 is a lysosomal/endosomal protein that is trafficked through the endoplasmic reticulum (ER) and Golgi. Furthermore, studies are required to confirm whether CLN3 has a potential role in the recycling of synaptic vesicles through the endosome/lysosome.

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Expression Studies of CLN3 Protein (Battenin) in Fusion with the Green Fluorescent Protein in Mammalian Cellsin Vitro

Cited by 34 publications

References 14 publications

Stable expression and visualization of Mat-8 (FXYD-3) tagged with a fluorescent protein in Chinese Hamster Ovary (CHO)-K1 cells

Stable expression and visualization of Mat-8 (FXYD-3) tagged with a fluorescent protein in Chinese Hamster Ovary (CHO)-K1 cells

Interactions of the proteins of neuronal ceroid lipofuscinosis: clues to function

Localization and processing of CLN3, the protein associated to batten disease: Where is it and what does it do?

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