Entry - *601747 - TRIPARTITE MOTIF-CONTAINING PROTEIN 23; TRIM23 - OMIM
 
* 601747

TRIPARTITE MOTIF-CONTAINING PROTEIN 23; TRIM23


Alternative titles; symbols

ADP-RIBOSYLATION FACTOR DOMAIN PROTEIN 1; ARFD1; ARD1
ARF DOMAIN PROTEIN 1


HGNC Approved Gene Symbol: TRIM23

Cytogenetic location: 5q12.3     Genomic coordinates (GRCh38): 5:65,589,690-65,624,333 (from NCBI)


TEXT

Description

TRIM23 belongs to the ADP-ribosylation factor (ARF) family of GTPases and contains an N-terminal GTPase-activating protein (GAP) domain and a C-terminal ARF domain (Vitale et al., 2000).


Cloning and Expression

Mishima et al. (1993) isolated a gene referred to as ARD1 from human and rat cDNA libraries. ARD1 encodes a putative 64-kD protein that contains an 18-kD ADP-ribosylation factor domain at the carboxyl terminus and is much larger than the other monomeric guanine nucleotide-binding ARF proteins previously identified.


Gene Function

Vitale et al. (2000) found that cytohesin-1 (PSCD1; 182115) interacted with ARD1 in a yeast 2-hybrid screen of a human liver cDNA library. ARD1-GDP interacted well with cytohesin-1 but poorly with cytohesin-2 (PSCD2; 602488), and cytohesin-1 accelerated binding of a nonhydrolyzable GTP analog to ARD1. Mutation analysis showed that the effector region of the ARF domain of ARD1 interacted with the Sec7 domain of cytohesin-1. Physical association between these domains was highly dependent on experimental conditions, and a free Mg(2+) concentration that favored nucleotide release from ARD1 and accumulation of the nucleotide-free ARD1 form also favored interaction between ARD1 and cytohesin-1. In transfected COS-7 cells, ARD1 associated with vesicular structures concentrated around the nucleus and scattered throughout the cytoplasm, corresponding to Golgi and lysosomes, respectively. A constitutively GDP-bound form of ARD1 showed a similar distribution, whereas a constitutively GTP-bound form of ARD1 was concentrated close to the nucleus in a Golgi-like distribution only. Cytohesin-1 was distributed throughout the cell and was also present in the nucleus. When ARD1 or its GDP- and GTP-bound forms were coexpressed with cytohesin-1, only the GDP-bound form showed any change in distribution or colocalization with cytohesin-1. In 90% of cells coexpressing the proteins, the GDP-bound form of ARD1 was distributed throughout the cell, except for the nucleus, and largely colocalized with cytohesin-1. In less than 10% of cells coexpressing the proteins, the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.


Mapping

Gross (2014) mapped the TRIM23 gene to chromosome 5q12.3 based on an alignment of the TRIM23 sequence (GenBank AF230397) with the genomic sequence (GRCh37).


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 5/21/2014.

  2. Mishima, K., Tsuchiya, M., Nightingale, M. S., Moss, J., Vaughan, M. ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain. J. Biol. Chem. 268: 8801-8807, 1993. [PubMed: 8473324, related citations]

  3. Vitale, N., Pacheco-Rodriguez, G., Ferrans, V. J., Riemenschneider, W., Moss, J., Vaughan, M. Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J. Biol. Chem. 275: 21331-21339, 2000. [PubMed: 10748148, related citations] [Full Text]


Matthew B. Gross - updated : 05/21/2014
Patricia A. Hartz - updated : 3/13/2007
Creation Date:
Lori M. Kelman : 4/10/1997
mgross : 05/21/2014
mgross : 3/15/2007
mgross : 3/15/2007
terry : 3/13/2007
carol : 3/26/1999
joanna : 4/10/1997

* 601747

TRIPARTITE MOTIF-CONTAINING PROTEIN 23; TRIM23


Alternative titles; symbols

ADP-RIBOSYLATION FACTOR DOMAIN PROTEIN 1; ARFD1; ARD1
ARF DOMAIN PROTEIN 1


HGNC Approved Gene Symbol: TRIM23

Cytogenetic location: 5q12.3     Genomic coordinates (GRCh38): 5:65,589,690-65,624,333 (from NCBI)


TEXT

Description

TRIM23 belongs to the ADP-ribosylation factor (ARF) family of GTPases and contains an N-terminal GTPase-activating protein (GAP) domain and a C-terminal ARF domain (Vitale et al., 2000).


Cloning and Expression

Mishima et al. (1993) isolated a gene referred to as ARD1 from human and rat cDNA libraries. ARD1 encodes a putative 64-kD protein that contains an 18-kD ADP-ribosylation factor domain at the carboxyl terminus and is much larger than the other monomeric guanine nucleotide-binding ARF proteins previously identified.


Gene Function

Vitale et al. (2000) found that cytohesin-1 (PSCD1; 182115) interacted with ARD1 in a yeast 2-hybrid screen of a human liver cDNA library. ARD1-GDP interacted well with cytohesin-1 but poorly with cytohesin-2 (PSCD2; 602488), and cytohesin-1 accelerated binding of a nonhydrolyzable GTP analog to ARD1. Mutation analysis showed that the effector region of the ARF domain of ARD1 interacted with the Sec7 domain of cytohesin-1. Physical association between these domains was highly dependent on experimental conditions, and a free Mg(2+) concentration that favored nucleotide release from ARD1 and accumulation of the nucleotide-free ARD1 form also favored interaction between ARD1 and cytohesin-1. In transfected COS-7 cells, ARD1 associated with vesicular structures concentrated around the nucleus and scattered throughout the cytoplasm, corresponding to Golgi and lysosomes, respectively. A constitutively GDP-bound form of ARD1 showed a similar distribution, whereas a constitutively GTP-bound form of ARD1 was concentrated close to the nucleus in a Golgi-like distribution only. Cytohesin-1 was distributed throughout the cell and was also present in the nucleus. When ARD1 or its GDP- and GTP-bound forms were coexpressed with cytohesin-1, only the GDP-bound form showed any change in distribution or colocalization with cytohesin-1. In 90% of cells coexpressing the proteins, the GDP-bound form of ARD1 was distributed throughout the cell, except for the nucleus, and largely colocalized with cytohesin-1. In less than 10% of cells coexpressing the proteins, the GDP-bound form of ARD1 and cytohesin-1 colocalized in lysosomes.


Mapping

Gross (2014) mapped the TRIM23 gene to chromosome 5q12.3 based on an alignment of the TRIM23 sequence (GenBank AF230397) with the genomic sequence (GRCh37).


REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 5/21/2014.

  2. Mishima, K., Tsuchiya, M., Nightingale, M. S., Moss, J., Vaughan, M. ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain. J. Biol. Chem. 268: 8801-8807, 1993. [PubMed: 8473324]

  3. Vitale, N., Pacheco-Rodriguez, G., Ferrans, V. J., Riemenschneider, W., Moss, J., Vaughan, M. Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). J. Biol. Chem. 275: 21331-21339, 2000. [PubMed: 10748148] [Full Text: https://doi.org/10.1074/jbc.M909642199]


Contributors:
Matthew B. Gross - updated : 05/21/2014
Patricia A. Hartz - updated : 3/13/2007

Creation Date:
Lori M. Kelman : 4/10/1997

Edit History:
mgross : 05/21/2014
mgross : 3/15/2007
mgross : 3/15/2007
terry : 3/13/2007
carol : 3/26/1999
joanna : 4/10/1997