scholarly journals The involvement of immunoglobulin superfamily proteins in spermatogenesis and sperm-egg interaction

2006 ◽  
Vol 5 (2) ◽  
pp. 87-93
Author(s):  
Kiyotata Toshimori ◽  
Mamiko Maekawa ◽  
Chizuru Ito ◽  
Yoshiro Toyama ◽  
Fumie Suzuki-Toyota ◽  
...  
Keyword(s):  
Immunoglobulin Superfamily ◽  
Immunoglobulin Superfamily Proteins

scholarly journals Molecular basis of synaptic specificity by immunoglobulin superfamily receptors in Drosophila

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Shouqiang Cheng ◽  
James Ashley ◽  
Justyna D Kurleto ◽  
Meike Lobb-Rabe ◽  
Yeonhee Jenny Park ◽  
...  
Keyword(s):  
Axon Guidance ◽  
Molecular Basis ◽  
Surface Proteins ◽  
Synaptic Connectivity ◽  
Immunoglobulin Superfamily ◽  
Neuronal Connectivity ◽  
Cell Surface Proteins ◽  
Synaptic Specificity ◽  
Immunoglobulin Superfamily Proteins ◽  
Synapse Targeting

In stereotyped neuronal networks, synaptic connectivity is dictated by cell surface proteins, which assign unique identities to neurons, and physically mediate axon guidance and synapse targeting. We recently identified two groups of immunoglobulin superfamily proteins in Drosophila, Dprs and DIPs, as strong candidates for synapse targeting functions. Here, we uncover the molecular basis of specificity in Dpr–DIP mediated cellular adhesions and neuronal connectivity. First, we present five crystal structures of Dpr–DIP and DIP–DIP complexes, highlighting the evolutionary and structural origins of diversification in Dpr and DIP proteins and their interactions. We further show that structures can be used to rationally engineer receptors with novel specificities or modified affinities, which can be used to study specific circuits that require Dpr–DIP interactions to help establish connectivity. We investigate one pair, engineered Dpr10 and DIP-α, for function in the neuromuscular circuit in flies, and reveal roles for homophilic and heterophilic binding in wiring.

scholarly journals The involvement of immunoglobulin superfamily proteins in spermatogenesis and sperm-egg interaction

2006 ◽  
Vol 5 (2) ◽  
pp. 87-93
Author(s):  
KIYOTATA TOSHIMORI ◽  
MAMIKO MAEKAWA ◽  
CHIZURU ITO ◽  
YOSHIRO TOYAMA ◽  
FUMIE SUZUKI-TOYOTA ◽  
...  
Keyword(s):  
Immunoglobulin Superfamily ◽  
Immunoglobulin Superfamily Proteins

Widespread expressions of immunoglobulin superfamily proteins in cancer cells

2011 ◽  
Vol 61 (1) ◽  
pp. 89-99 ◽  
Author(s):  
Gregory Lee ◽  
Mingang Zhu ◽  
Bixia Ge ◽  
Suzanne Potzold
Keyword(s):  
Cancer Cells ◽  
Immunoglobulin Superfamily ◽  
Immunoglobulin Superfamily Proteins

Lachesin: an immunoglobulin superfamily protein whose expression correlates with neurogenesis in grasshopper embryos

Development ◽  
1993 ◽  
Vol 118 (2) ◽  
pp. 509-522 ◽  
Author(s):  
R.O. Karlstrom ◽  
L.P. Wilder ◽  
M.J. Bastiani
Keyword(s):  
Fruit Fly ◽  
The Body ◽  
Developmental Expression ◽  
Immunoglobulin Superfamily ◽  
Glycosyl Phosphatidylinositol ◽  
Surface Recognition ◽  
Poliovirus Receptor ◽  
Mother Cells ◽  
Immunoglobulin Superfamily Proteins ◽  
Immunoglobulin Superfamily Protein

We describe the developmental expression in grasshopper (Schistocerca americana) and molecular characterization in grasshopper and fruit fly (Drosophila melanogaster) of Lachesin, a novel immunoglobulin superfamily protein. Lachesin is expressed on the surfaces of differentiating neuronal cells from the onset of neurogenesis in both the central and peripheral nervous systems. Lachesin expression begins in some cells of the neurogenic ectoderm immediately after engrailed expression begins in the posterior cells of each future segment. All neurogenic cells express Lachesin early, but only those cells that become neuroblasts continue to express Lachesin. Ectodermal cells in the neurogenic region that adopt non-neuronal fates lose Lachesin at the time that they diverge from a potentially neurogenic pathway. Neuroblasts, ganglion mother cells and neurons all express Lachesin early in their lives, but expression becomes restricted to a subset of neurons as development progresses. Sensory neurons express Lachesin as they delaminate from the body wall ectoderm. Lachesin is also present on growing axons of the CNS and PNS and becomes restricted to a subset of axons later in development. This expression is unique among known insect neurogenic genes and suggests a role for Lachesin in early neuronal differentiation and axon outgrowth. Grasshopper Lachesin is a 38 × 10(3) M(r) protein linked to cell membranes through a glycosyl phosphatidylinositol anchor. We have cloned the Lachesin gene from both grasshopper and fly. The proteins are highly conserved (70% identical) between the two species. Lachesin is similar to Drosophila amalgam, bovine OBCAM and the human poliovirus receptor, putting it into a subgroup of the immunoglobulin superfamily containing one V- and two C2-type immunoglobulin domains. Lachesin is also similar to several other vertebrate immunoglobulin superfamily proteins (TAG-1, F11, L1 and NgCAM) known to function in neurite outgrowth and other cell surface recognition events.

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