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Cullin family proteins and tumorigenesis: genetic association and molecular mechanisms.

Chen Z, Sui J, Zhang F, Zhang C - J Cancer (2015)

Bottom Line: Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors.These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression.Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types.

View Article: PubMed Central - PubMed

Affiliation: 1. Orthopedics Department, Changhai Hospital Affiliated to Second Military Medical University, Shanghai, China, 200433.

ABSTRACT
Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors. These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression. Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types. Over the past few years, our understanding of cullin proteins and their functions in genome stability and tumorigenesis has expanded enormously. Herein, this review briefly provides current perspectives on cullin protein functions, and mainly summarizes and discusses molecular mechanisms of cullin proteins in tumorigenesis.

No MeSH data available.


Related in: MedlinePlus

The domain structures of human cullin proteins. Numbers represent the amino acid codons. The blue lines indicate the position of the neddylation site 5.
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Figure 1: The domain structures of human cullin proteins. Numbers represent the amino acid codons. The blue lines indicate the position of the neddylation site 5.

Mentions: Cullins are evolutionarily conserved family proteins throughout bacteria, plants and mammals 1. The human genome encodes six cullin proteins characterized by a cullin homology (CH) domain in the carboxyl (C)-terminal, including CUL1, 2, 3, 4A, 4B and 5 (Figure 1) 2. Moreover, the human genome also encodes another two atypical cullin proteins (CUL7 and CUL9) that consist of additional homology domains 3, such as DOC1 (destruction of cyclin B) homology domain and IBR (in-between-ring) domain 3. These cullin proteins potentially assemble RING-box protein 1 (RBX1, also known as ROC1) and/or RBX2 (also known as ROC2 or SAG-sensitive to apoptosis gene), forming Cullin-RING ubiquitin ligases (CRLs) 4.


Cullin family proteins and tumorigenesis: genetic association and molecular mechanisms.

Chen Z, Sui J, Zhang F, Zhang C - J Cancer (2015)

The domain structures of human cullin proteins. Numbers represent the amino acid codons. The blue lines indicate the position of the neddylation site 5.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4317758&req=5

Figure 1: The domain structures of human cullin proteins. Numbers represent the amino acid codons. The blue lines indicate the position of the neddylation site 5.
Mentions: Cullins are evolutionarily conserved family proteins throughout bacteria, plants and mammals 1. The human genome encodes six cullin proteins characterized by a cullin homology (CH) domain in the carboxyl (C)-terminal, including CUL1, 2, 3, 4A, 4B and 5 (Figure 1) 2. Moreover, the human genome also encodes another two atypical cullin proteins (CUL7 and CUL9) that consist of additional homology domains 3, such as DOC1 (destruction of cyclin B) homology domain and IBR (in-between-ring) domain 3. These cullin proteins potentially assemble RING-box protein 1 (RBX1, also known as ROC1) and/or RBX2 (also known as ROC2 or SAG-sensitive to apoptosis gene), forming Cullin-RING ubiquitin ligases (CRLs) 4.

Bottom Line: Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors.These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression.Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types.

View Article: PubMed Central - PubMed

Affiliation: 1. Orthopedics Department, Changhai Hospital Affiliated to Second Military Medical University, Shanghai, China, 200433.

ABSTRACT
Cullin family proteins function as scaffolds to form numerous E3 ubiquitin ligases with RING proteins, adaptor proteins and substrate recognition receptors. These E3 ligases further recognize numerous substrates to participate in a variety of cellular processes, such as DNA damage and repair, cell death and cell cycle progression. Clinically, cullin-associated E3 ligases have been identified to involve numerous human diseases, especially with regard to multiple cancer types. Over the past few years, our understanding of cullin proteins and their functions in genome stability and tumorigenesis has expanded enormously. Herein, this review briefly provides current perspectives on cullin protein functions, and mainly summarizes and discusses molecular mechanisms of cullin proteins in tumorigenesis.

No MeSH data available.


Related in: MedlinePlus