1997
DOI: 10.1074/jbc.272.8.5175
|View full text |Cite
|
Sign up to set email alerts
|

Targeting of SCG10 to the Area of the Golgi Complex Is Mediated by Its NH2-terminal Region

Abstract: SCG10 is a neuronal growth-associated protein that is concentrated in the growth cones of developing neurons. SCG10 shows a high degree of sequence homology to the ubiquitous phosphoprotein stathmin, which has been recently identified as a factor that destabilizes microtubules by increasing their catastrophe rate. Whereas stathmin is a soluble cytosolic protein, SCG10 is membrane-associated, indicating that the protein acts in a distinct subcellular compartment. Identifying the precise intracellular distributi… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

6
89
0

Year Published

1997
1997
2010
2010

Publication Types

Select...
8

Relationship

3
5

Authors

Journals

citations
Cited by 91 publications
(95 citation statements)
references
References 32 publications
6
89
0
Order By: Relevance
“…It is, therefore, of interest that SCGlO and RB3 were both recovered in the particulate fraction and were thus most likely membrane bound, whereas stathmin is essentially cytosoluble [ l ] ; SCGlO was further shown to be present in the perinuclear region and in growth cones and is probably a vesicle-associated protein [36]. As the sequences of SCGIO and RB3RB3' do not contain any feature of a transmembrane protein, it is likely that RB3/RB3' are indeed palmitoylated in the cell as has been recently shown for SCGlO [44], and that this posttranslational modification contributes to their partial membrane association. This specific subcellular localization might participate in the functional specificity of the SCGIO and RB3/RB3' proteins, as compared to stathmin.…”
Section: Discussionmentioning
confidence: 95%
See 1 more Smart Citation
“…It is, therefore, of interest that SCGlO and RB3 were both recovered in the particulate fraction and were thus most likely membrane bound, whereas stathmin is essentially cytosoluble [ l ] ; SCGlO was further shown to be present in the perinuclear region and in growth cones and is probably a vesicle-associated protein [36]. As the sequences of SCGIO and RB3RB3' do not contain any feature of a transmembrane protein, it is likely that RB3/RB3' are indeed palmitoylated in the cell as has been recently shown for SCGlO [44], and that this posttranslational modification contributes to their partial membrane association. This specific subcellular localization might participate in the functional specificity of the SCGIO and RB3/RB3' proteins, as compared to stathmin.…”
Section: Discussionmentioning
confidence: 95%
“…However, no hydrophobic sequence of sufficient length for membrane spanning was identified within this A domain, but two closely located conserved cysteins at positions 20 and 22 within the A domain of SCGlO might constitute a palmitoylation site [44] (for a review, see [45]) responsible for its partial membrane binding. These two cystein residues are also conserved within the N-terminal A domain of RB3/RB3' (Figs 2, 3), as well as in the Xenopus XB3 sequence [34], which suggests that the RB3 and RB3' proteins are, as is SCG10, at least partially membrane Identification of protein forms.…”
Section: Rb3/rb3' C a C T C C T T G T G A C T T T T G G T C A A T T Cmentioning
confidence: 99%
“…22,30,31 In the present study, we assessed both the trafficking and cellular distribution of SCG10 in HSCs. To detect endogenous SCG10, we used an existing antibody for SCG10 which was highly specific in Western blot and immunofluorescence.…”
Section: In Situ Localization Of Scg10 and The Trafficking Pathway Inmentioning
confidence: 99%
“…The N-terminal region of SCG10 (amino acids 1-34) was thought to be important for membrane association, and the removal of this region re-http://bmbreports.org sulted in a soluble protein (∆SCG10) that is closely homologous to conventional stathmin (9). Thus, an N-terminal truncated GST-tagged form of ∆SCG10 was constructed to facilitate the purification of SCG10.…”
Section: Bri3 and Scg10 Associate In Vitro And In Vivomentioning
confidence: 99%
“…SCG10 is a microtubule-destabilizing protein that induces microtubule depolymerization in vitro and when overexpressed in cultured cells (9,12).…”
Section: Effects Of Bri3 and Scg10 Co-expression On Microtubule Organmentioning
confidence: 99%