+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1



Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1



Journal of Neuroscience 19(15): 6519-6527



Neuropilin-1 (Npn-1), a receptor for semaphorin III, mediates the guidance of growth cones on extending neurites. The molecular mechanism of Npn-1 signaling remains unclear. We have used a yeast two-hybrid system to isolate a protein that interacts with the cytoplasmic domain of Npn-1. This Npn-1-interacting protein (NIP) contains a central PSD-95/Dlg/ZO-1 (PDZ) domain and a C-terminal acyl carrier protein domain. The physiological interaction of Npn-1 and NIP is supported by co-immunoprecipitation of these two proteins in extracts from a heterologous expression system and from a native tissue. The C-terminal three amino acids of Npn-1 (S-E-A-COOH), which is conserved from Xenopus to human, is responsible for interaction with the PDZ domain-containing C-terminal two-thirds of NIP. NIP as well as Npn-1 are broadly expressed in mice as assayed by Northern and Western analysis. Immunohistochemistry and in situ hybridization experiments revealed that NIP expression overlaps with that of Npn-1. NIP has been independently cloned as RGS-GAIP-interacting protein (GIPC), where it was identified by virtue of its interaction with the C terminus of RGS-GAIP and suggested to participate in clathrin-coated vesicular trafficking. We suggest that NIP and GIPC may participate in regulation of Npn-1-mediated signaling as a molecular adapter that couples Npn-1 to membrane trafficking machinery in the dynamic axon growth cone.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 010335487

Download citation: RISBibTeXText

PMID: 10414980


Related references

Cloning and Characterization of Neuropilin-1-Interacting Protein: A Psd-95/Dlg/Zo-1 Domain-Containing Protein That Interacts with the Cytoplasmic Domain of Neuropilin-1. The Journal of Neuroscience 19(15): 6519-6527, 1999

A 30 kDa protein containing a PDZ domain binds to the cytoplasmic domains of neuropilin-1 and neuropilin-2. Molecular Biology of the Cell 10(SUPPL ): 41a, 1999

Crystal Structure of the Neuropilin-1 MAM Domain: Completing the Neuropilin-1 Ectodomain Picture. Structure 24(11): 2008-2015, 2016

Neuropilin-1-VEGFR-2 complexing requires the PDZ-binding domain of neuropilin-1. Journal of Biological Chemistry 283(37): 25110-4, 2008

The neuropilin 1 cytoplasmic domain is required for VEGF-A-dependent arteriogenesis. Developmental Cell 25(2): 156-168, 2013

The cytoplasmic domain of neuropilin-1 regulates focal adhesion turnover. Febs Letters 587(21): 3392-3399, 2014

Cloning and characterization of BAP3 (BAI-associated protein 3), a C2 domain-containing protein that interacts with BAI1. Biochemical and Biophysical Research Communications 251(1): 158-165, 1998

Cloning and characterization of BAI-associated protein 1: a PDZ domain-containing protein that interacts with BAI1. Biochemical and Biophysical Research Communications 247(3): 597-604, 1998

The cytoplasmic domain of Kit ligand interacts with cellular proteins through a PDZ domain on the target protein. Blood 98(11 Part 1): 797a-798a, November 16, 2001

Identification of BAIAP2 (BAI-associated protein 2), a novel human homologue of hamster IRSp53, whose SH3 domain interacts with the cytoplasmic domain of BAI1. Cytogenetics and Cell Genetics 84(1-2): 75-82, 1999

Identification of Baiap2 (Bai-associated protein 2), a novel human homologue of hamster Irsp53, whose Sh3 domain interacts with the cytoplasmic domain of Bai1. Cytogenetic and Genome Research 84(1-2): 75-82, 1999

Cloning and characterization of mCRIP2, a mouse LIM-only protein that interacts with PDZ domain IV of PTP-BL. Genes to Cells 8(7): 631-644, 2003

Characterization of ANKRA, a novel ankyrin repeat protein that interacts with the cytoplasmic domain of megalin. Journal of the American Society of Nephrology 11(12): 2167-2178, 2000

The cytoplasmic domain of neuropilin 1 is dispensable for angiogenesis, but promotes the spatial separation of retinal arteries and veins. Development 138(19): 4185-4191, 2011

Detailed characterization of the O-linked glycosylation of the neuropilin-1 c/MAM-domain. Glycoconjugate Journal 33(3): 387-397, 2017