Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal  proximal tubular cells

Pribanic, Sandra; Gisler, Serge M.; Bačić, Desa; Madjdpour, Caveh; Hernando, Nati; Sorribas, Vı́ctor; Gantenbein, Andrea; Biber, Jürg; Murer, Heini

doi:10.1152/ajprenal.00109.2003

Cited by 55 publications

(60 citation statements)

References 27 publications

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“…Because the previously reported interaction between MAP17 and NaPiIIa (28) was not detected during the screening of the mouse kidney cDNA library, we directly tested the NaPiIIa cDNA as well as several other relevant cDNA preys for interaction with MAP17 baits in the OK cell two-hybrid system (Table 2 and Fig. 1).…”

Section: Identification Of Proteins That Interact With Map17mentioning

confidence: 99%

“…Yeast two-hybrid experiments using the COOH-terminus end of MAP17 showed that this protein interacts specifically with NHERF3. These assays failed to find interactions with other PDZ-containing proteins (6,13,28).…”

mentioning

confidence: 99%

“…In addition, several proteins interact with NaPiIIa independently of PDZ domains. For example, MAP17 DD96/SPAP is a small membrane protein that interacts with the NH 2 terminus of the phosphate transporter (28). MAP17 was first identified by differential display because its RNA was overexpressed in several carcinomas (18).…”

mentioning

confidence: 99%

“…The reduction in NHERF3 levels was due to an increase in its degradation through a proteasome-independent mechanism. However, expression of MAP17 in opossum kidney (OK) cells did not modify the pattern of expression of NaPiIIa, nor the magnitude or nature of its adaptations to low or high phosphate concentrations, nor its response to parathyroid hormone (28).…”

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confidence: 99%

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Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

Lanaspa¹,

Giral²,

Breusegem³

et al. 2007

American Journal of Physiology-Renal Physiology

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.-The function of the NaPiIIa renal sodium-phosphate transporter is regulated through a complex network of interacting proteins. Several PDZ domain-containing proteins interact with its COOH terminus while the small membrane protein MAP17 interacts with its NH 2 end. To elucidate the function of MAP17, we identified its interacting proteins using both bacterial and mammalian two-hybrid systems. Several PDZ domain-containing proteins, including the four NHERF proteins, as well as NaPiIIa and NHE3, were found to bind to MAP17. The interactions of MAP17 with the NHERF proteins and with NaPiIIa were further analyzed in opossum kidney (OK) cells. Expression of MAP17 alone had no effect on the NaPiIIa apical membrane distribution, but coexpression of MAP17 and NHERF3 or NHERF4 induced internalization of NaPiIIa, MAP17, and the PDZ protein to the trans-Golgi network (TGN). This effect was not observed when MAP17 was cotransfected with NHERF1/2 proteins. Inhibition of protein kinase C (PKC) prevented expression of the three proteins in the TGN. Activation of PKC in OK cells transfected only with MAP17 induced complete degradation of MAP17 and NaPiIIa. When lysosomal degradation was prevented, both proteins accumulated in the TGN. When the dopamine D1-like receptor was activated with fenoldopam, both NaPiIIa and MAP17 also accumulated in the TGN. Finally, cotransfection of MAP17 and NHERF3 prevented the adaptive upregulation of phosphate transport activity in OK cells in response to low extracellular phosphate. Therefore, the interaction between MAP17, NHERF3/4, and NaPiIIa in the TGN could be an important intermediate or alternate path in the internalization of NaPiIIa. phosphate transport; PDZ; PDZK1; protein interaction; opossum kidney cells RENAL REABSORPTION OF INORGANIC phosphate (P i ) and its regulation involve molecular mechanisms more complicated than initially thought. After expression cloning of NaPiIIa (24), the transporter responsible for most renal P i reabsorption, a complex network of interacting proteins that modulate the activity of this transporter has been described (for reviews, see Refs. 4,5,15,35).Most of the proteins that interact with this transporter contain one or more PDZ domains (acronym of the postsynaptic density protein PSD-95, the Drosophila junctional protein Disc-large, and the tight junction protein ZO1). These domains consist of 80 -90 amino acids that very often (but not always) scaffold specific proteins into supramolecular complexes (17). Several PDZ domain-containing proteins interact with the COOH end of NaPiIIa (12) DD96/SPAP is a small membrane protein that interacts with the NH 2 terminus of the phosphate transporter (28). MAP17 was first identified by differential display because its RNA was overexpressed in several carcinomas (18). In addition, it was also isolated during the expression cloning of a renal Na/D-mannose cotransport in Xenopus laevis oocytes, and it was considered to be an activator of a mannose transporter endogenous to the oocyte (6). Yeast two-hybrid experi...

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Section: Identification Of Proteins That Interact With Map17mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

Lanaspa¹,

Giral²,

Breusegem³

et al. 2007

American Journal of Physiology-Renal Physiology

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“…MAP17 binds several PDZ domain-containing proteins, including PDZK1, NHERF proteins, NaPiIIa and NHe3. Together with NHRF3 and NHRF4, overexpression of MAP17 in opossum kidney cells leads to internalization of NaPilla to the trans-Golgi network (Pribanic et al, 2003;Lanaspa et al, 2007). The physiological role of MAP17 in proximal tubules is not known, but it stimulates specific Na-dependent transport of mannose and glucose in Xenopus oocytes (Blasco et al, 2003) and mammary cells (Guijarro et al, 2007a).…”

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confidence: 99%

p38α limits the contribution of MAP17 to cancer progression in breast tumors

et al. 2012

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MAP17 is a small, 17-kDa, non-glycosylated membrane protein that is overexpressed in a percentage of carcinomas. In the present work, we have analyzed the role of MAP17 expression during mammary cancer progression. We have found that MAP17 is expressed in 60% human mammary tumors while it is not expressed in normal or benign neoplasias. MAP17 levels increased with breast tumor stage and were strongly correlated with mammary tumoral progression. A significant increase in the levels of reactive oxygen species (ROS) was observed in MAP17-expressing cells, as compared with parental cells. This increase was further paralleled by an increase in the tumorigenic capacity of carcinoma cells but not in immortal non-tumoral breast epithelial cells, which provides a selective advantage once tumorigenesis has begun. Expression of specific MAP17 shRNA in proteinexpressing tumor cells reduced their tumorigenic capabilities, which suggests that this effect is dependent upon MAP17 protein expression. Our data show that ROS functions as a second messenger that enhances tumoral properties, which are inhibited in non-tumoral cells. We have found that p38a activation mediates this response. MAP17 triggers a ROS-dependent, senescence-like response that is abolished in the absence of p38a activation. Furthermore, in human breast tumors, MAP17 activation is correlated with a lack of phosphorylation of p38a. Therefore, MAP17 is overexpressed in late-stage breast tumors, in which oncogenic activity relies on p38 insensitivity to induce intracellular ROS.

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The Na⁺‐coupled glucose transporter SGLT2 interacts with its accessory unit MAP17 in vitro and their expressions overlap in the renal proximal tubule

Calado

Santos²,

Aires

et al. 2018

FEBS Letters

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Na -glucose cotransporter 2 is the renal Na -coupled glucose transporter responsible for the tubular glucose reabsorption, while MAP17 was recently identified as its accessory unit. Mutations in either of the proteins' coding genes, SLC5A2 and PDZK1IP1, lead to urinary glucose excretion. To investigate whether MAP17 interacts with SGLT2 in vitro, we engineered a V5-tagged SGLT2 construct and evaluated HEK293T cells coexpressing it together with a HA tagged MAP17 construct. MAP17 is shown to colocalize and coimmunoprecipitate with SGLT2. Also, in human kidney sections, the expression of both proteins overlaps at the apical surface of tubular epithelia. This interaction provides the rationale behind SGLT2 activation by MAP17 as well the similarity of the SLC5A2 and PDZK1IP1 glucosuric phenotypes.

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Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells

Cited by 55 publications

References 27 publications

Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

p38α limits the contribution of MAP17 to cancer progression in breast tumors

The Na⁺‐coupled glucose transporter SGLT2 interacts with its accessory unit MAP17 in vitro and their expressions overlap in the renal proximal tubule

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Interactions of MAP17 with the NaPi-IIa/PDZK1 protein complex in renal proximal tubular cells

Cited by 55 publications

References 27 publications

Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

Interaction of MAP17 with NHERF3/4 induces translocation of the renal Na/Pi IIa transporter to thetrans-Golgi

p38α limits the contribution of MAP17 to cancer progression in breast tumors

The Na+‐coupled glucose transporter SGLT2 interacts with its accessory unit MAP17 in vitro and their expressions overlap in the renal proximal tubule

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The Na⁺‐coupled glucose transporter SGLT2 interacts with its accessory unit MAP17 in vitro and their expressions overlap in the renal proximal tubule