Generation of divergent uroplakin tetraspanins and their partners during vertebrate evolution: identification of novel uroplakins

DeSalle, Rob; Chicote, Javier U.; Sun, Tung‐Tien; Garcı́a-España, Antonio

doi:10.1186/1471-2148-14-13

Cited by 22 publications

(36 citation statements)

References 48 publications

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“…Uroplakins (UPKs) are integral membrane proteins belonging to two families: UPK1a (UPIa) and UPK1b (UPIb) are members of the four-transmembrane domain tetraspanin (TSPAN or TM4SF) family [1,2]; and the single-spanning transmembrane uroplakins UPK2a (also known as UPII, encoded by the UPK2 gene), UPK2b (non-mammalian vertebrates), UPK3a (UPIIIa, UPK3A), UPK3b (UPIIIb, UPK3B), UPK3c (UPK3BL; present in mammals, reptiles and birds) and UPK3d (bony fish) form the tetraspanin-associated uroplakin family, UPK2/3 [3–7]. …”

Section: Introductionmentioning

confidence: 99%

“…Their protein structure, function and involvement in urinary tract development and malformations are the subject of several reports and reviews [5,7,9–16]. …”

Section: Introductionmentioning

confidence: 99%

“…In a previous report, we showed that both the tetraspanin uroplakins and the UPK2/3 families first appeared in the common ancestor of vertebrates [7]. While the origin of UPK1a and UPK1b can be explained by gene duplication from an ancestor invertebrate tetraspanin gene [2,5,17], the origin of the UPK2/3 family is not yet established as it does not appear to be related to any known protein family [7].…”

Section: Introductionmentioning

confidence: 99%

“…Specifically, PTPRQ belongs to subtype R3 phospho-tyrosine phosphatase receptors (R3 PTPRs), which like UPK2/3 uroplakins are single-spanning membrane proteins. However they are much larger than UPK2/3 proteins, which consist of an extracellular moiety of less than 200 amino acids and a short cytoplasmic tail, absent in UPK2a and UPK2b [3,7,20]. R3 PTPRs have a single cytoplasmic catalytic phophotyrosine phosphatase (PTP) domain and an extracellular region composed exclusively by fibronectin type III (FN3) domains (9 to 19 in humans).…”

Section: Introductionmentioning

confidence: 99%

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The Tetraspanin-Associated Uroplakins Family (UPK2/3) Is Evolutionarily Related to PTPRQ, a Phosphotyrosine Phosphatase Receptor

et al. 2017

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Uroplakins are a widespread group of vertebrate integral membrane proteins that belong to two different families: UPK1a and UPK1b belong to the large tetraspanin (TSPAN) gene family, and UPK3a, UPK3b, UPK3c, UPK3d, UPK2a and UPK2b form a family of their own, the UPK2/3 tetraspanin-associated family. In a previous study, we reported that uroplakins first appeared in vertebrates, and that uroplakin tetraspanins (UPK1a and UPK1b) should have originated by duplication of an ancestor tetraspanin gene. However, the evolutionary origin of the UPK2/3 family remains unclear. In this study, we provide evidence that the UPK2/3 family originated by gene duplication and domain loss from a protoPTPRQ-like basal deuterostome gene. PTPRQs are members of the subtype R3 tyrosine phosphatase receptor (R3 PTPR) family, which are characterized by having a unique modular composition of extracellular fibronectin (FN3) repeats, a transmembrane helix, and a single intra-cytoplasmic phosphotyrosine phophatase (PTP) domain. Our assumption of a deuterostome protoPTPRQ-like gene as an ancestor of the UPK2/3 family by gene duplication and loss of its PTP and fibronectin (FN3) domains, excluding the one closest to the transmembrane helix, is based on the following: (i) phylogenetic analyses, (ii) the existence of an identical intron/exon gene pattern between UPK2/3 and the corresponding genetic region in R3 PTPRs, (iii) the conservation of cysteine patterns and protein motifs between UPK2/3 and PTPRQ proteins and, (iv) the existence in tunicates, the closest organisms to vertebrates, of two sequences related to PTPRQ; one with the full subtype R3 modular characteristic and another without the PTP domain but with a short cytoplasmic tail with some sequence similarity to that of UPK3a. This finding will facilitate further studies on the structure and function of these important proteins with implications in human diseases.

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Section: Introductionmentioning

confidence: 99%

“…Their protein structure, function and involvement in urinary tract development and malformations are the subject of several reports and reviews [5,7,9–16]. …”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The Tetraspanin-Associated Uroplakins Family (UPK2/3) Is Evolutionarily Related to PTPRQ, a Phosphotyrosine Phosphatase Receptor

et al. 2017

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“…UPIa and UPIb are tetraspanins, while UPII and UPIIIa are single-span proteins. Moreover, latest sequencing of genomes has shown the existence of three new UPII/UPIII family members: UPIIb, UPIIIc, and UPIIId (Desalle et al 2014). Urothelial plaques seem to reduce membrane permeability on more levels.…”

Section: Uroplakinsmentioning

confidence: 99%

Properties of the Urothelium that Establish the Blood–Urine Barrier and Their Implications for Drug Delivery

Lasič

Višnjar

Kreft

2015

Reviews of Physiology, Biochemistry and Pharmacology

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The primary function of the urinary bladder is to store and periodically release urine. How the urothelium prevents permeation of water, ions, solutes, and noxious agents back into the bloodstream and underlying tissues as well as serving as a sensor and transducer of physiological and nociceptive stimuli is still not completely understood, and thus its unique functional complexity remains to be fully elucidated. This article reviews the permeation routes across urothelium as demonstrated in extensive morphological and electrophysiological studies on in vivo and in vitro urothelia. We consider the molecular and morphological structures of urothelium and how they contribute to the impermeability of the blood-urine barrier. Based on the available data, the extremely low permeability properties of urothelium can be postulated. This remarkable impermeability is necessary for the normal functioning of all mammals, but at the same time represents limitations regarding the uptake of drugs. Therefore, the current progress to overcome this most resilient barrier in our body for drug therapy purposes is also summarized in this review.

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Molecular ultrastructure of the urothelial surface: Insights from a combination of various microscopic techniques

Zupančič

Romih

Robenek

et al. 2014

Microsc. Res. Tech.

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The urothelium forms the blood–urine barrier, which depends on the complex organization of transmembrane proteins, uroplakins, in the apical plasma membrane of umbrella cells. Uroplakins compose 16 nm intramembrane particles, which are assembled into urothelial plaques. Here we present an integrated survey on the molecular ultrastructure of urothelial plaques in normal umbrella cells with advanced microscopic techniques. We analyzed the ultrastructure and performed measurements of urothelial plaques in the normal mouse urothelium. We used field emission scanning electron microscopy (FESEM), atomic force microscopy (AFM), transmission electron microscopy (TEM) on immunolabeled ultrathin sections (immuno‐TEM), and freeze‐fracture replicas (FRIL). We performed immunolabeling of uroplakins for scanning electron microscopy (immuno‐FESEM). All microscopic techniques revealed a variability of urothelial plaque diameters ranging from 332 to 1179 nm. All immunolabeling techniques confirmed the presence of uroplakins in urothelial plaques. FRIL showed the association of uroplakins with 16 nm intramembrane particles and their organization into plaques. Using different microscopic techniques and applied qualitative and quantitative evaluation, new insights into the urothelial apical surface molecular ultrastructure have emerged and may hopefully provide a timely impulse for many ongoing studies. The combination of various microscopic techniques used in this study shows how these techniques complement one another. The described advantages and disadvantages of each technique should be considered for future studies of molecular and structural membrane specializations in other cells and tissues. Microsc. Res. Tech. 77:896–901, 2014. © 2014 Wiley Periodicals, Inc.

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Generation of divergent uroplakin tetraspanins and their partners during vertebrate evolution: identification of novel uroplakins

Cited by 22 publications

References 48 publications

The Tetraspanin-Associated Uroplakins Family (UPK2/3) Is Evolutionarily Related to PTPRQ, a Phosphotyrosine Phosphatase Receptor

The Tetraspanin-Associated Uroplakins Family (UPK2/3) Is Evolutionarily Related to PTPRQ, a Phosphotyrosine Phosphatase Receptor

Properties of the Urothelium that Establish the Blood–Urine Barrier and Their Implications for Drug Delivery

Molecular ultrastructure of the urothelial surface: Insights from a combination of various microscopic techniques

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