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Analysis of the subcellular distribution of avian p95-APP2, an ARF-GAP orthologous to mammalian paxillin kinase linker.
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- Author(s): Paris S;Paris S; Za L; Sporchia B; de Curtis I
- Source:
The international journal of biochemistry & cell biology [Int J Biochem Cell Biol] 2002 Jul; Vol. 34 (7), pp. 826-37.
- Publication Type:
Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
- Language:
English
- Additional Information
- Source:
Publisher: Elsevier Country of Publication: Netherlands NLM ID: 9508482 Publication Model: Print Cited Medium: Print ISSN: 1357-2725 (Print) Linking ISSN: 13572725 NLM ISO Abbreviation: Int J Biochem Cell Biol Subsets: MEDLINE
- Publication Information:
Publication: Amsterdam : Elsevier
Original Publication: Exeter, England ; Tarrytown, NY, U.S.A. : Pergamon, c1995-
- Subject Terms:
- Abstract:
We describe here the identification and characterization of avian p95-APP2, a multi-domain protein of a recently identified family of ADP-ribosylation factor (ARF)-GTPase-activating proteins (GAPs) including mammalian G protein-coupled receptor kinases (GRK)-interactor 1 (GIT1), paxillin kinase linker (PKL), and GIT2, as well as avian p95-APP1. The p95-APP2 is eluted from Rac-GTP-gamma-S, but not from Rac-GDP-beta-S columns. As other members of the family, p95-APP2 has binding regions for the focal adhesion protein paxillin, and for the Rac exchanging factor PIX. Sequence comparison indicates that p95-APP2 is the avian orthologue of mammalian PKL. Expression studies showed a largely diffuse distribution of the full length p95-APP2, without evident effects on cell morphology. We observed a dramatic difference between the localization of the amino-terminal portion of the protein, including the ARF-GAP domain and the three ankyrin repeats, and the carboxy-terminal portion including the paxillin-binding site. Moreover, the expression of truncated carboxy-terminal polypeptides including both the PIX- and paxillin-binding regions leads to a marked localization of the protein together with paxillin at large vesicles. Comparison of the expression of corresponding ARF-GAP-deficient constructs from p95-APP2 and p95-APP1 shows their distribution at distinct endocytic compartments. Altogether, these data support a role of distinct members of this family of ARF-GAPs in the regulation of different steps of membrane traffic during cell motility, and suggest that p95-APP2 may shuttle between an intracellular compartment and the cell periphery, although, further work will be needed to address this point.
- Accession Number:
0 (Adaptor Proteins, Signal Transducing)
0 (Carrier Proteins)
0 (Cell Cycle Proteins)
0 (DNA, Complementary)
0 (GIT1 protein, human)
0 (GTPase-Activating Proteins)
0 (Macromolecular Substances)
0 (Phosphoproteins)
EC 3.6.5.2 (ADP-Ribosylation Factors)
- Publication Date:
Date Created: 20020416 Date Completed: 20020731 Latest Revision: 20190922
- Publication Date:
20221213
- Accession Number:
10.1016/s1357-2725(02)00008-0
- Accession Number:
11950598
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