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CAPG (capping protein (actin filament), gelsolinlike)
Peeyush Kumar Singh, Ranjan Tamuli
Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati-781 039, Assam, India
(PKS, RT)
Published in Atlas Database: November 2009
Online updated version : http://AtlasGeneticsOncology.org/Genes/CAPGID44449ch2p11.html
DOI: 10.4267/2042/44837
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 2.0 France Licence.
© 2010 Atlas of Genetics and Cytogenetics in Oncology and Haematology
the position 27-75 (49), 148-188 (41), and 261-307
(47); and a nuclear localization signal (NES) 137-146
(10). Three natural variants, VAR-047776 (V41I),
VAR-047777 (R198W), and VAR-047778 (R335H)
have been reported.
Isoforms: Altogether 15 different isoforms (eight
complete, one COOH complete, and six partial) have
been predicted. Isoform jApr07 is annotated, contains
79 amino acids N-terminal to the first AUG.
Identity
Other names: AFCP; MCP
HGNC (Hugo): CAPG
Location: 2p11.2
DNA/RNA
Description
DNA size: 15.58 kb; mRNA size: 1220 bp; 10 exons.
Expression
Protein
Ubiquitously expressed; highly expressed in prostate,
lung, and kidney.
Description
Localisation
348 amino acids; 38.518 kDa.
CapG protein contains three gelsolin-like repeats in
Cytoplasmic (52.2%), cytoskeletal (21.7%), and
nuclear (13.0%), according to PSORT II prediction.
Atlas Genet Cytogenet Oncol Haematol. 2010; 14(9)
809
CAPG (capping protein (actin filament), gelsolin-like)
Singh PK, Tamuli R
Function
Ovarian carcinomas
CAPG encodes a member of the gelsolin/villin family
of actin-regulatory proteins that reversibly blocks
(capping) the barbed ends of F-actin filaments in a Ca
2+
and phosphoinositide-regulated manner, but does not
sever preformed actin filaments. Capping contributes to
the control of actin-based motility in non-muscle cells.
Dysregulation of actin-based motility is a prominent
factor in cell transformation and is probably associated
with carcinogenesis. CAPG is also involved in cell
signaling, receptor-mediated membrane ruffling, and
phagocytosis.
Disease
In a Swedish women population, CAPG was expressed
more in tumors among deceased patients than survivors
with ovarian carcinomas. The stage III serous papillary
adenocarcinomas of the ovary show higher CAPG
expression and this is possibly correlated with the
advance disease stage. Overexpression of CAPG
promotes aggressive tumor progression.
Pancreatic cancer
Note
Up regulation and multiple isoforms of CapG were
detected in pancreatic cancer tissue and cell lines. High
level of CapG protein may possibly play an important
role in pancreatic cancer cell motility and consequently
dissemination.
Homology
The percent identity below represents identity of CAPG
over an aligned region in UniGene.
- Pan troglodytes: 99.7 % (percentage identity)
- Macaca mulatta: 99.7%
- Mus musculus: 95.4%
- Rattus norvegicus: 92.8%
- Bos taurus: 91.1%
- Danio rerio: 61.7%
Ocular melanoma
Implicated in
Note
CapG, which is a unique regulator of the actin
cytoskeleton, is expressed in malignant melanomas of
the uvea but not to a significant extent in normal uveal
melanocytes.
Breast cancer
Tumorigenic progression in cell lines
Disease
CAPG is expressed at higher levels in metastasizing
breast cancer, than in normal breast epithelium.
Furthermore, CapG protein is also transported more
rapidly into the nucleus of the breast cancerous cells
than the corresponding benign cells. CapG knockdown
reduces invasiveness in Matrigel invasion assay, which
supports the role of CAPG in cell motility. Thus,
increased expression of CAPG leads to dysregulation
of cell motility that promotes tumor invasion.
Note
Expression of the CapG protein was lost in the
tumorigenic cell line, isolated from a human diploid
fibroblast lineage. The CapG protein expression was
lost also in cancer cell lines including stomach cancer,
lung cancer and melanoma. The human stomach cancer
cell line AZ 521 became non-tumorigenic after the
introduction of CapG cDNA. Moreover, CapG
expression was repressed in small-cell lung cancer
tissues. These results indicate that CapG is a tumor
suppressor gene involved in the tumorigenic
progression of certain cancers.
Oral carcinogenesis
Note
Significant overexpression of CapG protein was
detected in oral squamous-cell carcinoma cells
(OSCCs) and oral premalignant lesions (OPLs).
Enhanced expression of CapG was also associated with
large tumour size and advanced staging of OSCCs.
Therefore, CapG may initiate or activate the neoplastic
process of OSCC cells including the regulation of
biologic behaviour of aggressive forms of cells rather
than as a suppressor.
Atlas Genet Cytogenet Oncol Haematol. 2010; 14(9)
References
Dabiri GA, Young CL, Rosenbloom J, Southwick FS. Molecular
cloning of human macrophage capping protein cDNA. A unique
member of the gelsolin/villin family expressed primarily in
macrophages. J Biol Chem. 1992 Aug 15;267(23):16545-52
Van Ginkel PR, Gee RL, Walker TM, Hu DN, Heizmann CW,
Polans AS. The identification and differential expression of
calcium-binding proteins associated with ocular melanoma.
Biochim Biophys Acta. 1998 Dec 10;1448(2):290-7
810
CAPG (capping protein (actin filament), gelsolin-like)
Singh PK, Tamuli R
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tumorigenicity, but not anchorage independence, of human
cancer cells by new candidate tumor suppressor gene CapG.
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Invasive breast cancer cells exhibit increased mobility of the
actin-binding protein CapG. Int J Cancer. 2008 Apr
1;122(7):1476-82
Thompson CC, Ashcroft FJ, Patel S, Saraga G,
Vimalachandran D, Prime W, Campbell F, Dodson A, Jenkins
RE, Lemoine NR, Crnogorac-Jurcevic T, Yin HL, Costello E.
Pancreatic cancer cells overexpress gelsolin family-capping
proteins, which contribute to their cell motility. Gut. 2007
Jan;56(1):95-106
This article should be referenced as such:
Singh PK, Tamuli R. CAPG (capping protein (actin filament),
gelsolin-like). Atlas Genet Cytogenet Oncol Haematol. 2010;
14(9):809-811.
Nomura H, Uzawa K, Ishigami T, Kouzu Y, Koike H, Ogawara
K, Siiba M, Bukawa H, Yokoe H, Kubosawa H, Tanzawa H.
Atlas Genet Cytogenet Oncol Haematol. 2010; 14(9)
811