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Role of c-Maf in Chondrocyte Differentiation: A Review.

Hong E, Di Cesare PE, Haudenschild DR - Cartilage (2011)

Bottom Line: Chondrocyte differentiation in the growth plate is an important process for the longitudinal growth of endochondral bones.Mafs are a subfamily of the basic ZIP (bZIP) transcription factor superfamily, which act as key regulators of tissue-specific gene expression and terminal differentiation in many tissues.There is increasing evidence that c-Maf and its splicing variant Lc-Maf play a role in chondrocyte differentiation in a temporal-spatial manner.

View Article: PubMed Central - PubMed

Affiliation: University of California Davis Medical Center, Division of Orthopaedic Research, Department of Orthopaedic Surgery, Sacramento, CA, USA.

ABSTRACT
Chondrocyte differentiation in the growth plate is an important process for the longitudinal growth of endochondral bones. Sox9 and Runx2 are the most often-studied transcriptional regulators of the chondrocyte differentiation process, but the importance of additional factors is also becoming apparent. Mafs are a subfamily of the basic ZIP (bZIP) transcription factor superfamily, which act as key regulators of tissue-specific gene expression and terminal differentiation in many tissues. There is increasing evidence that c-Maf and its splicing variant Lc-Maf play a role in chondrocyte differentiation in a temporal-spatial manner. This review summarizes the functions of c-Maf in chondrocyte differentiation and discusses the possible role of c-Maf in osteoarthritis progression.

No MeSH data available.


Related in: MedlinePlus

Different types of c-Maf binding interactions. c-Maf can form homodimers as well as heterodimers with other bZIP transcription factors. In addition, several factors, including general transcription factors (TBP), cofactors (CBP), and specific transcription factors (Sox9), interact with c-Maf.
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fig2-1947603510377464: Different types of c-Maf binding interactions. c-Maf can form homodimers as well as heterodimers with other bZIP transcription factors. In addition, several factors, including general transcription factors (TBP), cofactors (CBP), and specific transcription factors (Sox9), interact with c-Maf.

Mentions: The Maf proteins dimerize with themselves and with other bZIP proteins through the leucine zipper domain. They can also interact with several non-bZIP factors.15,31-33 The Maf binding partners that have been identified so far are summarized in Table 1, and the various types of c-Maf binding interactions are illustrated diagrammatically in Figure 2. There is specificity in Maf dimerization, and the different binding interactions affect the transactivation function of the Maf proteins. However, the circumstances that determine the binding of Maf to its partners are not fully understood. The small Maf proteins, which do not dimerize with large Mafs, generally repress transcription when they form homodimers. In contrast, when they form heterodimers with other members of bZip proteins, they can activate or repress transcription of genes regulating many aspects of cellular differentiation.34,35 A heterodimeric partner of small Maf, the transcription factor nuclear factor E2 p45-related factor-2 (Nrf2), displays decreased expression during chondrocyte differentiation and inhibits numerous aspects of chondrocyte differentiation in vitro.36 This suggests the possibility that small Maf/Nrf2 heterodimers may be involved in the negative regulation of chondrocyte differentiation, although no expression data for small Mafs are available in chondrocytes. Large Mafs efficiently form homodimers both in vitro and in vivo. They also have the ability to form heterodimers with AP-1 family members in vitro, although heterodimers have not yet been detected in vivo.21In vitro, c-Maf and Nrl can form heterodimers with c-Fos and c-Jun.20 MafA can heterodimerize with c-Jun but not with c-Fos, whereas MafB can form heterodimers with c-Fos but not with c-Jun.37 Considering that Maf proteins are expressed in a wide variety of cells and tissues, it has been suggested that mixing and matching of dimeric partners might create specific complexes within cells to affect target gene expression and cell differentiation.38


Role of c-Maf in Chondrocyte Differentiation: A Review.

Hong E, Di Cesare PE, Haudenschild DR - Cartilage (2011)

Different types of c-Maf binding interactions. c-Maf can form homodimers as well as heterodimers with other bZIP transcription factors. In addition, several factors, including general transcription factors (TBP), cofactors (CBP), and specific transcription factors (Sox9), interact with c-Maf.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4300789&req=5

fig2-1947603510377464: Different types of c-Maf binding interactions. c-Maf can form homodimers as well as heterodimers with other bZIP transcription factors. In addition, several factors, including general transcription factors (TBP), cofactors (CBP), and specific transcription factors (Sox9), interact with c-Maf.
Mentions: The Maf proteins dimerize with themselves and with other bZIP proteins through the leucine zipper domain. They can also interact with several non-bZIP factors.15,31-33 The Maf binding partners that have been identified so far are summarized in Table 1, and the various types of c-Maf binding interactions are illustrated diagrammatically in Figure 2. There is specificity in Maf dimerization, and the different binding interactions affect the transactivation function of the Maf proteins. However, the circumstances that determine the binding of Maf to its partners are not fully understood. The small Maf proteins, which do not dimerize with large Mafs, generally repress transcription when they form homodimers. In contrast, when they form heterodimers with other members of bZip proteins, they can activate or repress transcription of genes regulating many aspects of cellular differentiation.34,35 A heterodimeric partner of small Maf, the transcription factor nuclear factor E2 p45-related factor-2 (Nrf2), displays decreased expression during chondrocyte differentiation and inhibits numerous aspects of chondrocyte differentiation in vitro.36 This suggests the possibility that small Maf/Nrf2 heterodimers may be involved in the negative regulation of chondrocyte differentiation, although no expression data for small Mafs are available in chondrocytes. Large Mafs efficiently form homodimers both in vitro and in vivo. They also have the ability to form heterodimers with AP-1 family members in vitro, although heterodimers have not yet been detected in vivo.21In vitro, c-Maf and Nrl can form heterodimers with c-Fos and c-Jun.20 MafA can heterodimerize with c-Jun but not with c-Fos, whereas MafB can form heterodimers with c-Fos but not with c-Jun.37 Considering that Maf proteins are expressed in a wide variety of cells and tissues, it has been suggested that mixing and matching of dimeric partners might create specific complexes within cells to affect target gene expression and cell differentiation.38

Bottom Line: Chondrocyte differentiation in the growth plate is an important process for the longitudinal growth of endochondral bones.Mafs are a subfamily of the basic ZIP (bZIP) transcription factor superfamily, which act as key regulators of tissue-specific gene expression and terminal differentiation in many tissues.There is increasing evidence that c-Maf and its splicing variant Lc-Maf play a role in chondrocyte differentiation in a temporal-spatial manner.

View Article: PubMed Central - PubMed

Affiliation: University of California Davis Medical Center, Division of Orthopaedic Research, Department of Orthopaedic Surgery, Sacramento, CA, USA.

ABSTRACT
Chondrocyte differentiation in the growth plate is an important process for the longitudinal growth of endochondral bones. Sox9 and Runx2 are the most often-studied transcriptional regulators of the chondrocyte differentiation process, but the importance of additional factors is also becoming apparent. Mafs are a subfamily of the basic ZIP (bZIP) transcription factor superfamily, which act as key regulators of tissue-specific gene expression and terminal differentiation in many tissues. There is increasing evidence that c-Maf and its splicing variant Lc-Maf play a role in chondrocyte differentiation in a temporal-spatial manner. This review summarizes the functions of c-Maf in chondrocyte differentiation and discusses the possible role of c-Maf in osteoarthritis progression.

No MeSH data available.


Related in: MedlinePlus