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jakmip1

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Official Full Name
janus kinase and microtubule interacting protein 1
Synonyms
JAKMIP1; janus kinase and microtubule interacting protein 1; janus kinase and microtubule-interacting protein 1; FLJ31564; Gababrbp; JAMIP1; MARLIN1; GABA B receptor binding protein; GABA-B receptor-binding protein; Jak and microtubule interacting protein 1; JAKMIP 1; JKIP1_HUMAN; Marlin 1; Marlin-1; Multiple alpha-helices and RNA-linker protein 1; Multiple coiled coil GABABR1 binding protein; OTTHUMP00000155144; OTTHUMP00000203209; OTTHUMP00000203210; OTTHUMP00000203212; OTTHUMP00000217225; OTTHUMP00000217781; multiple coiled-coil GABABR1-binding protein

Recent Research

Janus kinase and microtubule-interacting protein 1 (JAKMIP1) belongs to a family of three related genes conserved in vertebrates. It encodes a 73 kDa coiled-coil protein with a highly basic N-terminal region that targets the protein on microtubules and a C-terminal regulatory region that can be post-translationally by serine/threonine phosphorylation. JAKMIP1 is enriched in the mammalian central nervous system (CNS), but it is also present in lymphoid cells, testis and skeletal muscle. In the brain JAKMIP1 is neuronal specific, and abundant in dendrites and axons of discrete anatomical regions including the cerebral cortex, hippocampus, olfactory bulb, preoptic area, hypothalamus, medulla and cerebellum. JAKMIP1 was identified for its ability to bind the N-terminal band Ferzin-radixin-moesin (FERM) homology domain of Tyk2, a member of the Janus kinase (Jak) family of non-receptor tyrosine kinases, central elements of cytokine signaling cascade. Recently JAKMIP1 was also identified as an interacting partner of gamma aminobutirric acid B receptor1 (GABA B R1) and as a regulatory protein of GABA BR2 mRNA.

Some reports have shown that JAKMIP1 plays a role in various cell programs, such as cytoskeleton rearrangement, cell polarization, intracellular transport or even cell signaling activities. In particular, JAKMIP1 participates in polarized secretion in lymphocytes, JAKMIP1 associates to the cytoskeleton in neurites, which is required for the maintenance of an intact Golgi apparatus and its depletion produces the down-regulation of kinesin-1, a plus-end directed molecular motor with a central function in morphogenesis and migration. JAKMIP1 is a component of the protein networks that control morphogenesis and migration of cortical pyramidal neurons. In addition, JAKMIP1 is highly expressed in tumor samples than in normal tissues, and higher expression of this protein may activate Wnt signaling, increase the accumulation of beta-catenin and increase the proliferation of cancer cells. Autism spectrum disorder (ASD) is a heritable, common neurodevelopmental disorder with diverse genetic causes. Some reports have identified that JAKMIP1 as differentially expressed in patients with distinct syndromic forms of ASD, fragile X syndrome, and 15q duplication syndrome. It has been proved that numerous JAKMIP1 binding proteins were components of messenger ribonucleo protein (mRNP) granules and known interactors of fragile X mental retardation protein (FMRP) that includes DEAD box helicase 5, and the poly (A) binding protein cytoplasmic 1. It has been demonstrated that JAKMIP1 is an important regulator of neuronal translation, it associates with mRNP granules and actively translating ribosomes (Figure 1),the loss of JAKMIP1 dysregulates neuronal translation during synaptic development, affecting glutamatergic NMDAR signaling, and results in social deficits, stereotyped activity, abnormal postnatal vocalizations, and other autistic-like behaviors in the mouse. This suggests that the altered JAKMIP1 levels found in ASD patients and mouse models likely contribute to their behavioral phenotypes.

jakmip1 Figure 1. The Roles of JAKMIP1 in Neuronal Translation.

In addition, JAKMIP1 is a novel effector memory gene restraining T cell-mediated cytotoxicity, it can inhibit target cell killing. JAKMIP1 is absent in naive CD8+ and CD4+ T lymphocytes from peripheral blood but is highly expressed in Ag-experienced T cells. In a gene expression follow-up of the development of CMV-specific CD8+ response, JAKMIP1 emerged as one of the most highly up-regulated genes from primary infection to latent stage.

References:

  1. Penney J, et al. JAKMIP1: Translating the Message for Social Behavior. Neuron, 2015, 88(6):1070-1072.
  2. Jamee M,et al. JAKMIP1, a Novel Regulator of Neuronal Translation, Modulates Synaptic Function and Autistic-like Behaviors in Mouse. Neuron, 2015, 88(6):1173-1191.
  3. Guo M H, et al. Whole exome sequencing to identify genetic causes of short stature. Horm Res Paediatr, 2014, 82(1):44-52.