Regions of evolutionary conservation between the rat and human prohibitin-encoding genes

Altus, Michael S.; Wood, Carla M.; Stewart, David A.; Roskams, A. Jane; Friedman, Varda; Henderson, Toni; Owens, Garrison; Danner, David B.; Jupe, Eldon R.; Dell’Orco, Robert T.; Jk, McClung

doi:10.1016/0378-1119(95)00164-2

Cited by 22 publications

(11 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The genomic structure of human and rat PHB1 are similar with intron 2 and 3 being about 1 kb larger in the rat gene [23]. The PHB domain, which spans amino acid residues 26-187 is encoded by exon 3, 4 and 5 and it is these exons that are most highly conserved between Phb1 and Phb2.…”

Section: The Structure Of the Prohibitinsmentioning

confidence: 87%

The Prohibitins: emerging roles in diverse functions

Mishra

Murphy

2006

Journal of Cellular and Molecular Medicine

260

221

View full text Add to dashboard Cite

Prohibitin 1, (Phb1) has a molecular mass of ~30 kDa and is also known as B-cell receptor associated protein-32 (BAP32), whereas a related protein, prohibitin 2 (Phb2), sometimes referred to as prohibitone [1], B-cell receptor associated protein-37 (BAP37) [2] or repressor of estrogen receptor action (REA) [3] has a mass of ~37 kDa. For the purpose of this review we will use the nomenclature of Phb1 and Phb2. The prohibitin name is derived from an historical perspective and probably only relates to one of the many physiological roles of these proteins. A Phb1 cDNA was first isolated by differential hybridization to RNA from normal versus regenerating rat liver [4] and consequently Phb1 was proposed to be an inhibitor of cellular proliferation, hence the name prohibitin. The corresponding mRNA when microinjected into normal human diploid fibroblasts attenuated DNA synthesis. However it was subsequently shown that this effect was attributable to the 3' untranslated region of the AbstractThe prohibitins, Phb1 and Phb2 are highly conserved proteins in eukaryotic cells that are present in multiple cellular compartments. Initial investigations focused on the role of Phb1 as an inhibitor of cell proliferation hence the original name prohibitin. However both proteins appear to have a diverse range of functions and recent evidence suggests that the prohibitins have very similar but as yet only partially understood functions. In addition to their role as chaperone proteins in the mitochondria, and their ability to target to lipid rafts, their is now compelling evidence that both prohibitins are localized in the nucleus and can modulate transcriptional activity by interacting with various transcription factors, including the steroid hormone receptors, either directly or indirectly. In addition Phb1 and Phb2 are present in the circulation and can be internalized when added to cultured cells suggesting that the circulating prohibitins may have some regulatory role. This review presents some of the recent developments in prohibitin research and focuses on the similarities in the structure and function of these interesting proteins.

show abstract

Section: The Structure Of the Prohibitinsmentioning

confidence: 87%

The Prohibitins: emerging roles in diverse functions

Mishra

Murphy

2006

Journal of Cellular and Molecular Medicine

260

221

View full text Add to dashboard Cite

show abstract

“…The abundance of PHB mRNA is inversely related to markers of cellular proliferation in different cells and tissues (Hussain-Hakimjee et al, 2006; Jupe et al, 1995; Lumpkin et al, 1995; Miyamoto et al, 2001; Tanno et al, 1997). Comparative genomic alignment studies have shown that the human and rat PHB genes are similar except for intron 2 and 3, which is ~1 kb larger in the rat gene (Altus et al, 1995). The hPHB gene encodes ~30 kDa protein, also known as B-cell receptor associated protein-32 (BAP32) gene (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

“…In eukaryotes PHB and PHB2 have highly conserved PHB domains. The PHB protein is 54% homologous with PHB2 (Chowdhury et al, 2012; Gamble et al, 2007) and has a single amino acid difference between rodents and humans (Altus et al, 1995). Orthologues of the PHB gene have been identified in several organisms including bacteria (de Monbrison and Picot, 2002; Narsimhan et al, 1997), plants (Snedden and Fromm, 1997; Takahashi et al, 2003), Trypanosoma brucei (Welburn and Murphy, 1998), Saccharomyces cerevisiae (yeast) (Kirchman et al, 2003; Tatsuta et al, 2005), and Drosophila (Eveleth et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Prohibitin (PHB) roles in granulosa cell physiology

2015

View full text Add to dashboard Cite

Ovarian granulosa cells (GC) play an important role in the growth and development of the follicle in the process known as folliculogenesis. In the present review, we focus on the recent developments in prohibitin (PHB) research in relation to GC physiological functions. PHB is a member of highly conserved eukaryotic protein family containing the repressor of estrogen activity (REA)/stomatin/prohibitin/flotillin/HflK/C (SPFH) domain [also known as the PHB domain] found in divergent species from prokaryotes to eukaryotes. PHB is ubiquitously expressed either in circulating free form or is present in multiple cellular compartments including mitochondria, nucleus and plasma membrane. In mitochondria, PHB is anchored to the mitochondrial inner membrane (IMM), and form complexes with the ATPases Associated with diverse cellular Activities (m-AAA) proteases. PHB continuously shuttles between the mitochondria, cytosol and nucleus. In the nucleus, PHB interacts with various transcription factors and modulate transcriptional activity directly or through interactions with chromatin remodeling proteins. Multiple functions have been attributed to the mitochondrial and nuclear prohibitin complexes such as cellular differentiation, anti-proliferation, morphogenesis and maintaining the functional integrity of the mitochondria. However, to date, the regulation of PHB expression patterns and GC physiological functions are not completely understood.

show abstract

“…In humans, the PHB gene (hPhb) maps to chromosome 17q21.1 and spans ~11 kb with 7 exons (9). The human and rodent Phb genes are similar except for introns 2 and 3, which are approximately 1 kb larger in the rat gene (10). The human and rodent Phb gene encode approximately 30 kDa proteins that have a single amino acid difference ( Figure 1) (8).…”

Section: Prohibitinsmentioning

confidence: 99%

The emerging roles of prohibitins in folliculogenesis

Thompson¹

2012

Front Biosci

View full text Add to dashboard Cite

Prohibitins are members of a highly conserved eukaryotic protein family containing the stomatin/ prohibitin/flotillin/HflK/C (SPFH) domain [also known as the prohibitin (PHB) domain] found in divergent species from prokaryotes to eukaryotes. Prohibitins are found in unicellular eukaryotes, fungi, plants, animals and humans. Prohibitins are ubiquitously expressed and present in multiple cellular compartments including the mitochondria, nucleus, and the plasma membrane, and shuttles between the mitochondria, cytosol and nucleus. Multiple functions have been attributed to the mitochondrial and nuclear prohibitins, including cellular differentiation, anti-proliferation, and morphogenesis. In the present review, we focus on the recent developments in prohibitins research related to folliculogenesis. Based on current research findings, the data suggest that these molecules play important roles in modulating specific responses of granulose cells to follicle stimulating hormone (FSH) by acting at multiple levels of the FSH signal transduction pathway. Understanding the molecular mechanisms by which the intracellular signaling pathways utilize prohibitins in governing folliculogenesis is likely to result in development of strategies to overcome fertility disorders and suppress ovarian cancer growth. KeywordsProhibitins; PHB; PHB2; Repressor Of Estrogen Receptor Action; REA; mitochondria; nucleus; Review INTRODUCTIONUnderstanding the mechanisms underlying the growth and development of a competent follicle with the capacity to release a fertilizable oocyte is a major goal of reproductive biology, particularly, since female infertility is clearly a major public health issue. Ovarian granulosa cells (GCs) play an important physiological role in supporting the development and selection of the dominant follicle by controlling oocyte maturation and by producing the steroid hormones, estrogen (E 2 ) and progesterone (P 4 ) that are critical for maintenance of the ovarian cycle. Mammalian ovarian follicular development is tightly regulated by (1-6). Based on current research findings, the data suggest that these molecules play important roles in modulating specific responses of GCs to follicle stimulating hormone (FSH) by acting at multiple levels of the FSH signal transduction pathway. Understanding the molecular mechanisms by which the intracellular signaling pathways utilize prohibitins in governing folliculogenesis is likely to result in development of strategies to overcome fertility disorders and suppress ovarian cancer growth. In the last decade, significant progress has been made in analyzing the expression, distribution and in determining the specific roles that the PHB and REA play in mammalian reproductive physiology. In the present review, we summarize some of the recent developments in PHB and REA research related to folliculogenesis. PROHIBITINSProhibitins are members of an extensive evolutionarily conserved family of proteins which includes stomatins, plasma membrane proteins of Escherichia coli (HflKC), f...

show abstract

Regions of evolutionary conservation between the rat and human prohibitin-encoding genes

Cited by 22 publications

References 17 publications

The Prohibitins: emerging roles in diverse functions

The Prohibitins: emerging roles in diverse functions

Prohibitin (PHB) roles in granulosa cell physiology

The emerging roles of prohibitins in folliculogenesis

Contact Info

Product

Resources

About