Implementasi Permendagri Nomor 15 Tahun 2008 Tentang Pengarusutamaan Gender pada Jenjang Pendidikan Dasar di Kota Malang

Windra Rizkiyana1 & Wahyu Widodo21 Mahasiswa & 2Staf Pengajar Program Pasca Sarjana, Universitas Muhammadiyah MalangAlamat Korespondensi : Jl. Bandung No.1 MalangEmail: [email protected] education, still found a gender gap regarding both aspects of the expansion of educationalaccess and equity, quality and relevance of education and management. The purpose of this studywere: (1) describe the substance Permendagri No. 15 of 2008 on Gender Mainstreaming; (2) describethe implementation of Permendagri No. 15 of 2008 on Gender Mainstreaming in Elementary Educationin Malang; (3) Analyze the obstacles encountered in implementation Permendagri No. 15 of 2008 onGender Mainstreaming in Elementary Education in Malang. This type of research is a descriptiveanalysis, using a qualitative approach that is supported by a quantitative approach. And the techniquesof data acolllection through by interviews and the documents. Study sites are in Malang EducationDepartment. Analysis of the data used is descriptive analysis of qualitative and quantitative theorysupported by Gender Analysis Pathway (GAP), Content Analysis and Root Analysis. Implementationof Permendagri No 15 of 2008 about gender mainstreaming in basic education levels in Malang hasnot been optimal. These proved by the remains of gender inequality or gap that occurs in all threeaspects, that access and educational equity, quality and relevance of education, as well as accountabilityand governance. Constraints encountered in implementation Permendagri No. 15 of 2008 on gendermainstreaming in elementary education in Malang include: (a) Outreach activities that are specificallyabout the PUG in primary education has not been done; (b) The budget is not specifically formainstreaming activities; (c) newly formed working group PUG.Key word: Permendagri No. 15 of 2008, gender mainstreaming, basic educatio

Genetic analysis of the regulation of the voltage-gated calcium channel homolog Cch1 by the γ subunit homolog Ecm7 and cortical ER protein Scs2 in yeast

<div><p>The yeast Cch1/Mid1 Ca²⁺ channel is equivalent to animal voltage-gated Ca²⁺ channels and activated in cells incubated in low Ca²⁺ medium. We herein investigated the third subunit, Ecm7, under the same cell culture conditions. The deletion of <i>ECM7</i> slightly lowered Ca²⁺ influx activity in the <i>CNB1</i>⁺ background, in which calcineurin potentially dephosphorylates Cch1, but markedly lowered this activity in the <i>cnb1</i>Δ background. The deletion of the C-terminal cytoplasmic region of Ecm7 also reduced Ca²⁺ influx activity. We identified a novel Cch1-interacting protein, Scs2, which is known as a cortical endoplasmic reticulum membrane protein. The deletion of <i>SCS2</i> did not affect Ca²⁺ influx activity when calcineurin was inhibited by FK506, but enhanced this activity by 35% when the enzyme was not inhibited. However, this enhancement was canceled by the deletion of <i>ECM7</i>. These results suggest that Cch1/Mid1 is regulated differentially by Ecm7 and Scs2 in a manner that is dependent on the phosphorylation status of Cch1.</p></div

The deletion of <i>SCS2</i> increases Ca^<i>2+</i> accumulation in calcineurin-active cells, but not in calcineurin-inactivated cells.

<p>Experimental conditions and procedures were the same as those described in the legend to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0181436#pone.0181436.g002" target="_blank">Fig 2</a>. Cells were incubated for 2 h with 6 μM α-factor only (A) or with 6 μM α-factor and 2.0 μg/ml FK506 (B). *1, <i>p</i> < 0.05 (<i>scs2</i>Δ <i>vs</i>. WT); *2, <i>p</i> > 0.05 (<i>scs2</i>Δ <i>ecm7</i>Δ <i>vs</i>. <i>ecm7</i>Δ); *3, <i>p</i> > 0.05 (<i>scs2</i>Δ <i>vs</i>. WT); *4, <i>p</i> < 0.05 (<i>scs2</i>Δ <i>ecm7</i>Δ <i>vs</i>. <i>ecm7</i>Δ). Data are the mean ± SD of three independent experiments.</p

The deletion of <i>ECM7</i> and <i>CNB1</i> does not affect the amount of Cch1.

<p>Cells with various deletion mutations were exposed for 2 h to 6 μM α-factor and crude extracts were prepared. The amount of Cch1 in these cells was assessed by Western blotting. Enolase is an internal marker.</p

C-terminal truncations after amino acid residues 322 and 412 decrease Ecm7 activity.

<p>Experimental conditions and procedures were the same as those described in the legend to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0181436#pone.0181436.g002" target="_blank">Fig 2</a>. The positions of a deletion (Δ429–432) and small truncation (1–432) were also described under the graph. *1, <i>p</i> > 0.05 (<i>cnb1</i>Δ<i>/</i>vector <i>vs</i>. <i>ecm7</i>Δ <i>cnb1</i>Δ<i>/</i>mutated <i>ECM7s</i>); *2, <i>p</i> < 0.05 (<i>cnb1</i>Δ<i>/</i>vector <i>vs</i>. <i>ecm7</i>Δ <i>cnb1</i>Δ<i>/</i>mutated <i>ECM7s</i>). Data are the mean ± SD of three independent experiments.</p

Strains used in this study.

<p>Strains used in this study.</p

The deletion of <i>ECM7</i> results in a marked decrease in Ca²⁺ accumulation and viability in <i>cnb1</i>Δ cells.

<p>Experimental conditions and procedures were the same as those described in the legend to <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0181436#pone.0181436.g002" target="_blank">Fig 2</a>. *1, <i>p</i> < 0.05 (WT <i>vs</i>. <i>cnb1</i>Δ); *2, <i>p</i> < 0.05 (<i>cnb1</i>Δ <i>vs</i>. <i>cnb1</i>Δ <i>ecm7</i>Δ); *3, <i>p</i> < 0.05 (WT <i>vs</i>. <i>cnb1</i>Δ <i>ecm7</i>Δ); *4, <i>p</i> < 0.05 (WT <i>vs</i>. <i>cnb1</i>Δ); *5, <i>p</i> < 0.05 (<i>cch1</i>Δ <i>vs</i>. <i>cnb1</i>Δ <i>ecm7</i>Δ). Data are the mean ± SD of three independent experiments.</p

Plasmids used in this study.

<p>Plasmids used in this study.</p

Schematic diagram of Ecm7.

<p>This diagram was drawn based on transmembrane prediction with the TMHMM Server v 2.0 (<a href="http://www.cbs.dtu.dk/services/TMHMM/" target="_blank">http://www.cbs.dtu.dk/services/TMHMM/</a>). Circles represent phosphorylation sites determined by a mass spectrometry-based proteomic analysis [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0181436#pone.0181436.ref026" target="_blank">26</a>]. The red arrows represent cut sites to produce C-terminally truncated forms of Ecm7.</p

The deletion of <i>ECM7</i> results in a slight decrease in Ca²⁺ accumulation and viability in <i>CNB1</i>⁺ cells.

<p>Cells grown in SD.Ca100 medium were treated with 6 μM α-factor and incubated. Ca²⁺ accumulation and the viability of cells were assessed 2 h and 8 h after the addition of α-factor. *1, <i>p</i> < 0.05 (WT <i>vs</i>. <i>ecm7</i>Δ); *2, <i>p</i> > 0.05 (<i>cch1</i>Δ <i>vs</i>. <i>cch1</i>Δ <i>ecm7</i>Δ); *3, <i>p</i> < 0.05 (WT <i>vs</i>. <i>ecm7</i>Δ); *4, <i>p</i> < 0.05 (<i>cch1</i>Δ <i>vs</i>. <i>cch1</i>Δ <i>ecm7</i>Δ). Data are the mean ± SD of three independent experiments.</p