The bovine mannose 6-phosphate/insulin-like growth factor II receptor. The role of arginine residues in mannose 6-phosphate binding.

Dahms, Nancy M.; Rose, Pamela A.; Molkentin, Jeffery D.; Zhang, Yan; Brzycki, M. A.

doi:10.1016/s0021-9258(18)53343-3

Cited by 99 publications

(17 citation statements)

References 45 publications

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“…8 c, clone Dd4 cells transfected with a CIMPR lacking the intact sorting signal and impaired in lysosomal sorting (Lobel et al, 1989), exhibited a quite uniform staining for uPAR similar to that of the CIMPR-negative cells. Cells transfected with the clone Mut39 mutant CIMPR incapable of binding Man-6-P ligands as ␤-glucuronidase (Dahms et al, 1993), showed a staining pattern (Fig. 8 d) similar to that of clone Cc2 cells transfected with wild-type CIMPR.…”

Section: Cimpr Modulates the Subcellular Distribution Of Uparmentioning

confidence: 75%

“…Catalytically inactivated uPA (DFP-uPA), which binds to uPAR with the same affinity as uPA and pro-uPA, did not influence the binding reaction. On the other hand, the binding was clearly suppressed by ␤-glucuronidase, which binds to sites in repeats 3 and 9 in CIMPR via Man-6-P epitopes (Dahms et al, 1993). This may suggest a steric hindrance for binding of uPAR to CIMPR occupied with ␤-glucuronidase.…”

Section: Effect Of Ligands To Upar and Cimpr On The Binding Reactionmentioning

confidence: 97%

“…Murine L cells lacking CIMPR (clone D9) and L cells transfected with full-length CIMPR (clone Cc2) and a truncated receptor lacking 154 amino acids of the cytoplasmatic tail (clone Dd4) have been described before (Lobel et al, 1989). The D9 cell line transfected with a mutated CIMPR lacking intact Man-6-P binding sites (clone Mut39, Arg 435 to Ala and Arg 1,334 to Ala) (Dahms et al, 1993) was generously provided by Dr. N.M. Dahms, Medical College of Wisconsin (Milwaukee, WI). The D9 cell line transfected with the 46-kD, cation-dependent mannose 6-phosphate receptor (CDMPR) has been described (Johnson et al, 1990).…”

Section: Cell Linesmentioning

confidence: 99%

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Mannose 6-Phosphate/Insulin-like Growth Factor–II Receptor Targets the Urokinase Receptor to Lysosomes via a Novel Binding Interaction

Nykjær

Christensen²,

Vorum

et al. 1998

The Journal of Cell Biology

140

117

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The urokinase-type plasminogen activator receptor (uPAR) plays an important role on the cell surface in mediating extracellular degradative processes and formation of active TGF-β, and in nonproteolytic events such as cell adhesion, migration, and transmembrane signaling. We have searched for mechanisms that determine the cellular location of uPAR and may participate in its disposal. When using purified receptor preparations, we find that uPAR binds to the cation-independent, mannose 6-phosphate/insulin-like growth factor–II (IGF-II) receptor (CIMPR) with an affinity in the low micromolar range, but not to the 46-kD, cation-dependent, mannose 6-phosphate receptor (CDMPR). The binding is not perturbed by uPA and appears to involve domains DII + DIII of the uPAR protein moiety, but not the glycosylphosphatidylinositol anchor. The binding occurs at site(s) on the CIMPR different from those engaged in binding of mannose 6-phosphate epitopes or IGF-II. To evaluate the significance of the binding, immunofluorescence and immunoelectron microscopy studies were performed in transfected cells, and the results show that wild-type CIMPR, but not CIMPR lacking an intact sorting signal, modulates the subcellular distribution of uPAR and is capable of directing it to lysosomes. We conclude that a site within CIMPR, distinct from its previously known ligand binding sites, binds uPAR and modulates its subcellular distribution.

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Section: Cimpr Modulates the Subcellular Distribution Of Uparmentioning

confidence: 75%

Section: Effect Of Ligands To Upar and Cimpr On The Binding Reactionmentioning

confidence: 97%

Section: Cell Linesmentioning

confidence: 99%

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Mannose 6-Phosphate/Insulin-like Growth Factor–II Receptor Targets the Urokinase Receptor to Lysosomes via a Novel Binding Interaction

Nykjær

Christensen²,

Vorum

et al. 1998

The Journal of Cell Biology

140

117

View full text Add to dashboard Cite

show abstract

“…Gluco-II (ER glucosidase II β-subunit), GNPTase-γ (GlcNAcphosphotransferase γ-subunit). Repeats 3 and 9 of CI-MPR are shown as these are the ones involved in ligand binding [15].…”

mentioning

confidence: 99%

The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins

Munro

2001

Current Biology

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“…The exact locations of the binding sites for mannose 6-phosphate and IGF-II still need to be defined. Studies using truncated forms of the extracytoplasmic domain of the bovine M6PIIGF-II receptor indicate that for binding of mannose 6-phosphate repeats 1-3 and 7-9 (22,23), and for binding of IGF-II repeats 5-11 (24) are sufficient.…”

mentioning

confidence: 99%

Localization of the Insulin-like Growth Factor II Binding Site to Amino Acids 1508–1566 in Repeat 11 of the Mannose 6-Phosphate/Insulin-like Growth Factor II Receptor

Schmidt

Kiecke-Siemsen

Waheed

et al. 1995

Journal of Biological Chemistry

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The mannose 6-phosphate/insulin-like growth factor II receptor (M6P/IGF-II receptor) binds insulin-like growth factor II (IGF-II) with high affinity. To localize the IGF-II binding site within the 15 repeating units that form the extracytoplasmic domain of the receptor, purified human M6P/IGF-II receptor was digested with thermolysin, and the fragments were analyzed for their ability to bind 125I-IGF-II in a cross-linking assay. Two IGF-II-binding receptor fragments of 23 and 37 kDa were purified. Sequence analysis revealed that the fragments consist of disulfide connected peptides comprising amino acids 1331-1566 and 1331-1697 of the receptor repeats 9-12. In a second approach we expressed truncated forms of the M6P/IGF-II receptor fused to the C terminus of the extracytoplasmic domain of the 46-kDa mannose 6-phosphate receptor. Fusion proteins containing M6P/IGF-II receptor repeats 10-15, 10-11, or 11-15 bound IGF-II, whereas a fusion protein containing the single repeat 10 failed to bind. This result indicates that repeat 11 (amino acids 1508-1650) is sufficient for binding of IGF-II. Residues 1508-1566, which are shared by the 23-kDa IGF-II-binding fragment and repeat 11, are proposed to form the IGF-II binding site of the M6P/IGF-II receptor.

show abstract

The bovine mannose 6-phosphate/insulin-like growth factor II receptor. The role of arginine residues in mannose 6-phosphate binding.

Cited by 99 publications

References 45 publications

Mannose 6-Phosphate/Insulin-like Growth Factor–II Receptor Targets the Urokinase Receptor to Lysosomes via a Novel Binding Interaction

Mannose 6-Phosphate/Insulin-like Growth Factor–II Receptor Targets the Urokinase Receptor to Lysosomes via a Novel Binding Interaction

The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins

Localization of the Insulin-like Growth Factor II Binding Site to Amino Acids 1508–1566 in Repeat 11 of the Mannose 6-Phosphate/Insulin-like Growth Factor II Receptor

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